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Human Metabolome Database Version 2.5

 

Showing metabocard for Tetradecanoyl-CoA (HMDB01521)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:53
Accession Number HMDB01521
Secondary Accession Numbers HMDB06517
Common Name Tetradecanoyl-CoA
Description Tetradecanoyl-CoA (or myristoyl-CoA) is an intermediate in fatty acid biosynthesis, fatty acid elongation and the beta oxidation of fatty acids. It is also used in the myristoylation of proteins. The first pass through the beta-oxidation process starts with the saturated fatty acid palmitoyl-CoA and produces myristoyl-CoA. A total of four enzymatic steps are required, starting with VLCAD CoA dehydrogenase (Very Long Chain) activity, followed by three enzymatic steps catalyzed by enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and ketoacyl-CoA thiolase, all present in the mitochondria. Myristoylation of proteins is also catalyzed by the presence of myristoyl-CoA along with Myristoyl-CoA:protein N-myristoyltransferase (NMT). Myristoylation is an irreversible, co-translational (during translation) protein modification found in animals, plants, fungi and viruses. In this protein modification a myristoyl group (derived from myristioyl CoA) is covalently attached via an amide bond to the alpha-amino group of an N-terminal amino acid of a nascent polypeptide. It is more common on glycine residues but also occurs on other amino acids. Myristoylation also occurs post-translationally, for example when previously internal glycine residues become exposed by caspase cleavage during apoptosis. Myristoylation plays a vital role in membrane targeting and signal transduction in plant responses to environmental stress. Compared to other species that possess a single functional myristoyl-CoA: protein N-myristoyltransferase (NMT) gene copy, human, mouse and cow possess 2 NMT genes, and more than 2 protein isoforms.
Synonyms
  1. Myristoyl-CoA
  2. Myristoyl-coenzyme A
  3. S-Tetradecanoyl-coenzyme A
  4. n-C14:0CoA
  5. Tetradecanoyl CoA
  6. Tetradecanoyl-coenzyme A
  7. n-C14:0Coenzyme A
  8. Tetradecanoyl Coenzyme A
Chemical IUPAC Name [(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-2-[[hydroxy-[hydroxy-[3-hydroxy-2,2-dimethyl-3-[2-(2-tetradecanoylsulfanylethylcarbamoyl)ethylcarbamoyl]propoxy]phosphoryl]oxy-phosphoryl]oxymethyl]oxolan-3-yl]oxyphosphonic acid
Chemical Formula C35H62N7O17P3S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Coenzyme A Derivatives
Sub Class
  • Medium chain acyl CoAs
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • primary amine
  • primary aromatic amine
  • secondary carboxylic acid amide
  • thiocarboxylic acid ester
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Lipid biosynthesis, Fatty acid transport
Application
—
Source
  • Endogenous
Average Molecular Weight 977.890
Monoisotopic Molecular Weight 977.313599
Isomeric SMILES CCCCCCCCCCCCCC(=O)SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N
Canonical SMILES CCCCCCCCCCCCCC(=O)SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(O)(=O)OP(O)(=O)OCC1OC(C(O)C1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N
KEGG Compound ID C02593 Link Image
BioCyc ID TETRADECANOYL-COA Link Image
BiGG ID 40154 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01521 Link Image
Metagene Link HMDB01521 Link Image
METLIN ID 3707 Link Image
PubChem Compound 1126 Link Image
PubChem Substance 6450468 Link Image
ChEBI ID 15532 Link Image
CAS Registry Number 3130-72-1
InChI Identifier InChI=1/C35H62N7O17P3S/c1-4-5-6-7-8-9-10-11-12-13-14-15-26(44)63-19-18-37-25(43)16-17-38-33(47)30(46)35(2,3)21-56-62(53,54)59-61(51,52)55-20-24-29(58-60(48,49)50)28(45)34(57-24)42-23-41-27-31(36)39-22-40-32(27)42/h22-24,28-30,34,45-46H,4-21H2,1-3H3,(H,37,43)(H,38,47)(H,51,52)(H,53,54)(H2,36,39,40)(H2,48,49,50)/t24-,28-,29-,30?,34-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.21 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 1.84 [Predicted by ALOGPS]; -0.8 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1IIC Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location Not Available
Tissue Location
Tissue References
Fibroblasts —
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Beta Oxidation of Very Long Chain Fatty Acids SMP00052 Link Image map01040 Link Image
Fatty Acid Elongation In Mitochondria SMP00054 Link Image map00062 Link Image
Fatty acid Metabolism SMP00051 Link Image map00071 Link Image
Mitochondrial Beta-Oxidation of Long Chain Saturated Fatty Acids SMP00482 Link Image
General References
  1. Hunt MC, Ruiter J, Mooyer P, van Roermond CW, Ofman R, Ijlst L, Wanders RJ: Identification of fatty acid oxidation disorder patients with lowered acyl-CoA thioesterase activity in human skin fibroblasts. Eur J Clin Invest. 2005 Jan;35(1):38-46. [PubMed Link Image]
Metabolic Enzymes
  1. 3-ketoacyl-CoA thiolase, mitochondrial
  2. Trifunctional enzyme subunit beta, mitochondrial precursor
  3. Medium-chain specific acyl-CoA dehydrogenase, mitochondrial precursor
  4. Acyl-coenzyme A oxidase 1, peroxisomal
  5. Acyl-coenzyme A oxidase 3, peroxisomal
  6. Peroxisomal trans-2-enoyl-CoA reductase
  7. Glycylpeptide N-tetradecanoyltransferase 1
  8. Glycylpeptide N-tetradecanoyltransferase 2
  9. Acyl-Coenzyme A dehydrogenase, long chain
  10. ACAA1 protein
  11. cDNA FLJ76905, highly similar to Homo sapiens N-myristoyltransferase 1 (NMT1), mRNA (N-myristoyltransferase 1, isoform CRA_b)
  12. cDNA FLJ30111 fis, clone BNGH42000360, highly similar to 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16)
  13. Glycylpeptide N-tetradecanoyltransferase
  14. Glycylpeptide N-tetradecanoyltransferase
  15. Glycylpeptide N-tetradecanoyltransferase
  16. Glycylpeptide N-tetradecanoyltransferase
  17. Glycylpeptide N-tetradecanoyltransferase
  18. Glycylpeptide N-tetradecanoyltransferase
  19. Glycylpeptide N-tetradecanoyltransferase
Enzyme 1 [top]
Enzyme 1 ID 5260
Enzyme 1 Name 3-ketoacyl-CoA thiolase, mitochondrial
Enzyme 1 Synonyms
  1. Beta- ketothiolase
  2. Acetyl-CoA acyltransferase
  3. Mitochondrial 3-oxoacyl- CoA thiolase
  4. T1
Enzyme 1 Gene Name ACAA2
Enzyme 1 Protein Sequence >3-ketoacyl-CoA thiolase, mitochondrial 
MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVL
QSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTE
SMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECD
KYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFK
KDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAI
SGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSR
ITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA
Enzyme 1 Number of Residues 397
Enzyme 1 Molecular Weight 41925
Enzyme 1 Theoretical pI 8.21
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Lipid transport and metabolism
Enzyme 1 Specific Function Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Enzyme 1 Pathways
  • Benzoate Degradation via Hydroxylation (map00362 Link Image)
  • Bile Acid Biosynthesis (map00120 Link Image)
  • Fatty Acid Elongation In Mitochondria (map00062 Link Image)
  • Fatty Acid Metabolism (map00071 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 1 Reactions
  • acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-12
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 509676 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P42765 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name THIM_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1194 bp 
ATGCGTCTGCTCCGAGGTGTGTTTGTAGTTGCTGCTAAGCGAACGCCCTTTGGAGCTTAC
GGAGGCCTTCTGAAAGACTTCACTGCTACTGACTTGTCTGAATTTGCTGCCAAGGCTGCC
TTGTCTGCTGGCAAAGTCTCACCTGAAACAGTTGACAGTGTGATTATGGGCAATGTCCTG
CAGAGTTCTTCAGATGCTATATATTTGGCAAGGCATGTTGGTTTGCGTGTGGGAATCCCA
AAGGAGACCCCAGCTCTCACGATTAATAGGCTCTGTGGTTCTGGTTTTCAGTCCATTGTG
AATGGATGTCAGGAAATTTGTGTTAAAGAAGCTGAAGTTGTTTTATGTGGAGGAACCGAA
AGCATGAGCCAAGCTCCCTACTGTGTCAGAAATGTGCGTTTTGGAACCAAGCTTGGATCA
GATATCAAGCTGGAAGATTCTTTATGGGTATCATTAACAGATCAGCATGTCCAGCTCCCC
ATGGCAATGACTGCAGAGAATCTTACTGTAAAACACAAAATAAGCAGAGAAGAATGTGAC
AAATATGCCCTGCAGTCACAGCAGAGATGGAAAGCTGCTAATGATGCTGGCTACTTTAAT
GATGAAATGGCACCAATTGAAGTGAAGACAAAGAAAGGAAAACAGACAATGCAGGTAGAC
GAGCATGCTCGGCCCCAAACCACCCTGGAACAGTTACAGAAACTTCCTCCAGTATTCAAG
AAAGATGGAACTGTTACTGCAGGGAATGCATCGGGTGTAGCTGATGGTGCTGGAGCTGTT
ATCATAGCTAGTGAAGATGCTGTTAAGAAACATAACTTCACACCACTGGCAAGAATTGTG
GGCTACTTTGTATCTGGATGTGATCCCTCTATCATGGGTATTGGTCCTGTCCCTGCTATC
AGTGGGGCACTGAAGAAAGCAGGACTGAGTCTTAAGGACATGGATTTGGTAGAGGTGAAT
GAAGCTTTTGCTCCCCAGTACTTGGCTGTTGAGAGGAGTTTGGATCTTGACATAAGTAAA
ACCAATGTGAATGGAGGAGCCATTGCTTTGGGTCACCCACTGGGAGGATCTGGATCAAGA
ATTACTGCACACCTGGTTCACGAATTAAGGCGTCGAGGTGGAAAATATGCCGTTGGATCA
GCTTGCATTGGAGGTGGCCAAGGTATTGCTGTCATCATTCAGAGCACAGCCTGA
Enzyme 1 GenBank Gene ID D16294 Link Image
Enzyme 1 GeneCard ID ACAA2 Link Image
Enzyme 1 GenAtlas ID ACAA2 Link Image
Enzyme 1 HGNC ID HGNC:83 Link Image
Enzyme 1 Chromosome Location 18
Enzyme 1 Locus 18q21.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Abe H, Ohtake A, Yamamoto S, Satoh Y, Takayanagi M, Amaya Y, Takiguchi M, Sakuraba H, Suzuki Y, Mori M, et al.: Cloning and sequence analysis of a full length cDNA encoding human mitochondrial 3-oxoacyl-CoA thiolase. Biochim Biophys Acta. 1993 Nov 16;1216(2):304-6. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5277
Enzyme 2 Name Trifunctional enzyme subunit beta, mitochondrial precursor
Enzyme 2 Synonyms
  1. TP-beta[Includes: 3-ketoacyl-CoA thiolase
  2. Acetyl-CoA acyltransferase
  3. Beta-ketothiolase]
Enzyme 2 Gene Name HADHB
Enzyme 2 Protein Sequence >Trifunctional enzyme subunit beta, mitochondrial precursor 
MTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAPAVQTKTKKTLAKPNIRNVVVVDGV
RTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAA
LGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMR
KLMLDLNKAKSMGQRLSLISKFRFNFLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLE
QDEYALRSHSLAKKAQDEGLLSDVVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPY
GTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATP
KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNW
GGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYPK
Enzyme 2 Number of Residues 474
Enzyme 2 Molecular Weight 51295
Enzyme 2 Theoretical pI 9.94
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Lipid transport and metabolism
Enzyme 2 Specific Function Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Enzyme 2 Pathways
  • Benzoate Degradation via Hydroxylation (map00362 Link Image)
  • Bile Acid Biosynthesis (map00120 Link Image)
  • Fatty Acid Elongation In Mitochondria (map00062 Link Image)
  • Fatty Acid Metabolism (map00071 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 2 Reactions
  • acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 862458 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P55084 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ECHB_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1425 bp 
ATGACTATCTTGACTTACCCCTTTAAAAATCTTCCCACTGCATCAAAATGGGCCCTCAGA
TTTTCCATAAGACCTCTGAGCTGTTCCTCCCAGCTACGAGCTGCCCCAGCTGTCCAGACC
AAAACGAAGAAGACGTTAGCCAAACCCAATATAAGGAATGTTGTGGTGGTGGATGGTGTT
CGCACTCCATTTTTGCTGTCTGGCACTTCATATAAAGACCTGATGCCACATGATTTGGCT
AGAGCAGCGCTTACGGGTTTGTTGCATCGGACCAGTGTCCCTAAGGAAGTAGTTGATTAT
ATCATCTTTGGTACAGTTATTCAGGAAGTGAAAACAAGCAATGTGGCTAGAGAGGCTGCC
CTTGGAGCTGGCTTCTCTGACAAGACTCCTGCTCACACTGTCACCATGGCTTGTATCTCT
GCCAACCAAGCCATGACCACAGGTGTTGGCTTGATTGCTTCTGGCCAGTGTGATGTGATC
GTGGCAGGTGGTGTTGAGTTGATGTCCGATGTCCCTATTCGTCACTCAAGGAAAATGAGA
AAACTGATGCTTGATCTCAATAAGGCCAAATCTATGGGCCAGCGACTGTCTTTAATCTCT
AAATTCCGATTTAATTTCCTAGCACCTGAGCTCCCTGCGGTTTCTGAGTTCTCCACCAGT
GAGACCATGGGCCACTCTGCAGACCGACTGGCCGCTGCCTTTGCTGTTTCTCGGCTGGAA
CAGGATGAATATGCACTGCGCTCTCACAGTCTAGCCAAGAAGGCACAGGATGAAGGACTC
CTTTCTGATGTGGTACCCTTCAAAGTACCAGGAAAAGATACAGTTACCAAAGATAATGGC
ATCCGTCCTTCCTCACTGGAGCAGATGGCCAAACTAAAACCTGCATTCATCAAGCCCTAC
GGCACAGTGACAGCTGCAAATTCTTCTTTCTTGACTGATGGTGCATCTGCAATGTTAATC
ATGGCGGAGGAAAAGGCTCTGGCCATGGGTTATAAGCCGAAGGCATATTTGAGGGATTTT
ATGTATGTGTCTCAGGATCCAAAAGATCAACTATTACTTGGACCAACATATGCTACTCCA
AAAGTTCTAGAAAAGGCAGGATTGACCATGAATGATATTGATGCTTTTGAATTTCATGAA
GCTTTCTCGGGTCAGATTTTGGCAAATTTTAAAGCCATGGATTCTGATTGGTTTGCAGAA
AACTACATGGGTAGAAAAACCAAGGTTGGATTGCCTCCTTTGGAGAAGTTTAATAACTGG
GGTGGATCTCTGTCCCTGGGACACCCATTTGGAGCCACTGGCTGCAGGTTGGTCATGGCT
GCTGCCAACAGATTACGGAAAGAAGGAGGCCAGTATGGCTTAGTGGCTGCGTGTGCAGCT
GGAGGGCAGGGCCATGCTATGATAGTGGAAGCTTATCCAAAATAA
Enzyme 2 GenBank Gene ID D16481 Link Image
Enzyme 2 GeneCard ID HADHB Link Image
Enzyme 2 GenAtlas ID HADHB Link Image
Enzyme 2 HGNC ID HGNC:4803 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 2p23
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Kamijo T, Aoyama T, Komiyama A, Hashimoto T: Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein. Biochem Biophys Res Commun. 1994 Mar 15;199(2):818-25. [PubMed Link Image]
  2. Orii KE, Aoyama T, Wakui K, Fukushima Y, Miyajima H, Yamaguchi S, Orii T, Kondo N, Hashimoto T: Genomic and mutational analysis of the mitochondrial trifunctional protein beta-subunit (HADHB) gene in patients with trifunctional protein deficiency. Hum Mol Genet. 1997 Aug;6(8):1215-24. [PubMed Link Image]
  3. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  4. Ushikubo S, Aoyama T, Kamijo T, Wanders RJ, Rinaldo P, Vockley J, Hashimoto T: Molecular characterization of mitochondrial trifunctional protein deficiency: formation of the enzyme complex is important for stabilization of both alpha- and beta-subunits. Am J Hum Genet. 1996 May;58(5):979-88. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5336
Enzyme 3 Name Medium-chain specific acyl-CoA dehydrogenase, mitochondrial precursor
Enzyme 3 Synonyms
  1. MCAD
Enzyme 3 Gene Name ACADM
Enzyme 3 Protein Sequence >Medium-chain specific acyl-CoA dehydrogenase, mitochondrial precursor 
MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEI
IPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ
TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKG
DEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNM
GQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEAT
KYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF
AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYK
N
Enzyme 3 Number of Residues 421
Enzyme 3 Molecular Weight 46589
Enzyme 3 Theoretical pI 8.51
Enzyme 3 GO Classification
Function
  • acyl-CoA dehydrogenase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function This enzyme is specific for acyl chain lengths of 4 to 16
Enzyme 3 Pathways
Enzyme 3 Reactions
  • acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 187433 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P11310 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ACADM_HUMAN Link Image
Enzyme 3 PDB ID 1T9G Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1266 bp 
ATGGCAGCGGGGTTCGGGCGATGCTGCAGGGTCCTGAGAAGTATTTCTCGTTTTCATTGG
AGATCACAGCATACAAAAGCCAATCGACAACGTGAACCAGGATTAGGATTTAGTTTTGAG
TTCACCGAACAGCAGAAAGAATTTCAAGCTACTGCTCGTAAATTTGCCAGAGAGGAAATC
ATCCCAGTGGCTGCAGAATATGATAAAACTGGTGAATATCCAGTCCCCCTAATTAGAAGA
GCCTGGGAACTTGGTTTAATGAACACACACATTCCAGAGAACTGTGGAGGTCTTGGACTT
GGAACTTTTGATGCTTGTTTAATTAGTGAAGAATTGGCTTATGGATGTACAGGGGTTCAG
ACTGCTATTGAAGGAAATTCTTTGGGGCAAATGCCTATTATTATTGCTGGAAATGATCAA
CAAAAGAAGAAGTATTTGGGGAGAATGACTGAGGAGCCATTGATGTGTGCTTATTGTGTA
ACAGAACCTGGAGCAGGCTCTGATGTAGCTGGTATAAAGACCAAAGCAGAAAAGAAAGGA
GATGAGTATATTATTAATGGTCAGAAGATGTGGATAACCAACGGAGGAAAAGCTAATTGG
TATTTTTTATTGGCACGTTCTGATCCAGATCCTAAAGCTCCTGCTAATAAAGCCTTTACT
GGATTCATTGTGGAAGCAGATACCCCAGGAATTCAGATTGGGAGAAAGGAATTAAACATG
GGCCAGCGATGTTCAGATACTAGAGGAATTGTCTTCGAAGATGTGAAAGTGCCTAAAGAA
AATGTTTTAATTGGTGACGGAGCTGGTTTCAAAGTTGCAATGGGAGCTTTTGATAAAACC
AGACCTGTAGTAGCTGCTGGTGCTGTTGGATTAGCACAAAGAGCTTTGGATGAAGCTACC
AAGTATGCCCTGGAAAGGAAAACTTTCGGAAAGCTACTTGTAGAGCACCAAGCAATATCA
TTTATGCTGGCTGAAATGGCAATGAAAGTTGAACTAGCTAGAATGAGTTACCAGAGAGCA
GCTTGGGAGGTTGATTCTGGTCGTCGAAATACCTATTATGCTTCTATTGCAAAGGCATTT
GCTGGAGATATTGCAAATCAGTTAGCTACTGATGCTGTGCAGATACTTGGAGGCAATGGA
TTTAATACAGAATATCCTGTAGAAAAACTAATGAGGGATGCCAAAATCTATCAGATTTAT
GAAGGTACTTCACAAATTCAAAGACTTATTGTAGCCCGTGAACACATTGACAAGTACAAA
AATTAA
Enzyme 3 GenBank Gene ID M91432 Link Image
Enzyme 3 GeneCard ID ACADM Link Image
Enzyme 3 GenAtlas ID ACADM Link Image
Enzyme 3 HGNC ID HGNC:89 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1p31
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Kelly DP, Kim JJ, Billadello JJ, Hainline BE, Chu TW, Strauss AW: Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and its expression in enzyme-deficient human tissue. Proc Natl Acad Sci U S A. 1987 Jun;84(12):4068-72. [PubMed Link Image]
  2. Matsubara Y, Narisawa K, Miyabayashi S, Tada K, Coates PM, Bachmann C, Elsas LJ 2nd, Pollitt RJ, Rhead WJ, Roe CR: Identification of a common mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency. Biochem Biophys Res Commun. 1990 Aug 31;171(1):498-505. [PubMed Link Image]
  3. Lee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJ: Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity. Biochemistry. 1996 Sep 24;35(38):12412-20. [PubMed Link Image]
  4. Tanaka K, Yokota I, Coates PM, Strauss AW, Kelly DP, Zhang Z, Gregersen N, Andresen BS, Matsubara Y, Curtis D, et al.: Mutations in the medium chain acyl-CoA dehydrogenase (MCAD) gene. Hum Mutat. 1992;1(4):271-9. [PubMed Link Image]
  5. Yokota I, Indo Y, Coates PM, Tanaka K: Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation. J Clin Invest. 1990 Sep;86(3):1000-3. [PubMed Link Image]
  6. Kelly DP, Whelan AJ, Ogden ML, Alpers R, Zhang ZF, Bellus G, Gregersen N, Dorland L, Strauss AW: Molecular characterization of inherited medium-chain acyl-CoA dehydrogenase deficiency. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9236-40. [PubMed Link Image]
  7. Yokota I, Coates PM, Hale DE, Rinaldo P, Tanaka K: Molecular survey of a prevalent mutation, 985A-to-G transition, and identification of five infrequent mutations in the medium-chain Acyl-CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency. Am J Hum Genet. 1991 Dec;49(6):1280-91. [PubMed Link Image]
  8. Gregersen N, Andresen BS, Bross P, Winter V, Rudiger N, Engst S, Christensen E, Kelly D, Strauss AW, Kolvraa S, et al.: Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli. Hum Genet. 1991 Apr;86(6):545-51. [PubMed Link Image]
  9. Blakemore AI, Singleton H, Pollitt RJ, Engel PC, Kolvraa S, Gregersen N, Curtis D: Frequency of the G985 MCAD mutation in the general population. Lancet. 1991 Feb 2;337(8736):298-9. [PubMed Link Image]
  10. Andresen BS, Jensen TG, Bross P, Knudsen I, Winter V, Kolvraa S, Bolund L, Ding JH, Chen YT, Van Hove JL, et al.: Disease-causing mutations in exon 11 of the medium-chain acyl-CoA dehydrogenase gene. Am J Hum Genet. 1994 Jun;54(6):975-88. [PubMed Link Image]
  11. Ziadeh R, Hoffman EP, Finegold DN, Hoop RC, Brackett JC, Strauss AW, Naylor EW: Medium chain acyl-CoA dehydrogenase deficiency in Pennsylvania: neonatal screening shows high incidence and unexpected mutation frequencies. Pediatr Res. 1995 May;37(5):675-8. [PubMed Link Image]
  12. Brackett JC, Sims HF, Steiner RD, Nunge M, Zimmerman EM, deMartinville B, Rinaldo P, Slaugh R, Strauss AW: A novel mutation in medium chain acyl-CoA dehydrogenase causes sudden neonatal death. J Clin Invest. 1994 Oct;94(4):1477-83. [PubMed Link Image]
  13. Andresen BS, Bross P, Udvari S, Kirk J, Gray G, Kmoch S, Chamoles N, Knudsen I, Winter V, Wilcken B, Yokota I, Hart K, Packman S, Harpey JP, Saudubray JM, Hale DE, Bolund L, Kolvraa S, Gregersen N: The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: is there correlation between genotype and phenotype? Hum Mol Genet. 1997 May;6(5):695-707. [PubMed Link Image]
  14. Kuchler B, Abdel-Ghany AG, Bross P, Nandy A, Rasched I, Ghisla S: Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site. Biochem J. 1999 Jan 15;337 ( Pt 2):225-30. [PubMed Link Image]
  15. Yang BZ, Ding JH, Zhou C, Dimachkie MM, Sweetman L, Dasouki MJ, Wilkinson J, Roe CR: Identification of a novel mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency. Mol Genet Metab. 2000 Mar;69(3):259-62. [PubMed Link Image]
  16. Andresen BS, Dobrowolski SF, O'Reilly L, Muenzer J, McCandless SE, Frazier DM, Udvari S, Bross P, Knudsen I, Banas R, Chace DH, Engel P, Naylor EW, Gregersen N: Medium-chain acyl-CoA dehydrogenase (MCAD) mutations identified by MS/MS-based prospective screening of newborns differ from those observed in patients with clinical symptoms: identification and characterization of a new, prevalent mutation that results in mild MCAD deficiency. Am J Hum Genet. 2001 Jun;68(6):1408-18. Epub 2001 May 8. [PubMed Link Image]
  17. Zschocke J, Schulze A, Lindner M, Fiesel S, Olgemoller K, Hoffmann GF, Penzien J, Ruiter JP, Wanders RJ, Mayatepek E: Molecular and functional characterisation of mild MCAD deficiency. Hum Genet. 2001 May;108(5):404-8. [PubMed Link Image]
  18. Albers S, Levy HL, Irons M, Strauss AW, Marsden D: Compound heterozygosity in four asymptomatic siblings with medium-chain acyl-CoA dehydrogenase deficiency. J Inherit Metab Dis. 2001 Jun;24(3):417-8. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5378
Enzyme 4 Name Acyl-coenzyme A oxidase 1, peroxisomal
Enzyme 4 Synonyms
  1. Palmitoyl-CoA oxidase
  2. AOX
  3. Straight-chain acyl-CoA oxidase
  4. SCOX
Enzyme 4 Gene Name ACOX1
Enzyme 4 Protein Sequence >Acyl-coenzyme A oxidase 1, peroxisomal 
MNPDLRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHEDLNFLTRSQRY
EVAVRKSAIMVKKMREFGIADPDEIMWFKKLHLVNFVEPVGLNYSMFIPTLLNQGTTAQK
EKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETQEFILNSPTVTSIKWWPGGL
GKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNGYL
KMDNHRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGEAARALSKACTIA
IRYSAVRHQSEIKPGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIG
QGDLSELPELHALTAGLKAFTSWTANTGIEACRMACGGHGYSHCSGLPNIYVNFTPSCTF
EGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYLNDLPSQRIQPQQVAVWPTMVDINSP
ESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFS
EKLLKIQDKAIQAVLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIR
SDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWAKNSPLNKAEVHESYKHLKSLQSKL
Enzyme 4 Number of Residues 660
Enzyme 4 Molecular Weight 74425
Enzyme 4 Theoretical pI 8.29
Enzyme 4 GO Classification
Function
  • FAD binding
  • acyl-CoA dehydrogenase activity
  • acyl-CoA oxidase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
  • purine nucleotide binding
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • electron transport
  • fatty acid beta-oxidation
  • fatty acid metabolism
  • fatty acid oxidation
  • generation of precursor metabolites and energy
  • metabolism
  • organic acid metabolism
  • physiological process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • microbody
  • organelle
  • peroxisome
Enzyme 4 General Function Lipid transport and metabolism
Enzyme 4 Specific Function Catalyzes the desaturation of very long chain acyl-CoAs to 2-trans-enoyl-CoAs
Enzyme 4 Pathways
Enzyme 4 Reactions
  • acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 458119 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q15067 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name ACOX1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1983 bp 
ATGAACCCGGACCTGCGCAGGGAGCGGGATTCCGCCAGCTTCAACCCGGAGCTGCTTACA
CACATCCTGGACGGCAGCCCCGAGAAAACGCGCCGCCGCCGAGAGATCGAGAACATGATC
CTGAACGACCCAGACTTCCAGCATGAGGACTTGAACTTCCTCACTCGCAGCCAGCGTTAT
GAGGTGGCTGTCAGGAAAAGTGCCATCATGGTGAAGAAGATGAGGGAGTTTGGCATCGCT
GACCCTGATGAAATTATGTGGTTTAAAAAACTACATTTGGTCAATTTTGTGGAACCTGTG
GGCCTCAATTACTCCATGTTTATTCCTACCTTGCTGAATCAGGGCACCACTGCTCAGAAA
GAGAAATGGCTGCTTTCATCCAAAGGACTCCAGATAATTGGCACCTACGCCCAGACGGAA
ATGGGCCACGGAACTCACCTTCGAGGCTTGGAAACCACAGCCACGTATGACCCTGAAACC
CAGGAGTTCATTCTCAACAGTCCTACTGTGACCTCCATTAAATGGTGGCCTGGTGGGCTT
GGAAAGACTTCAAATCATGCAATAGTTCTTGCCCAGCTCATCACTAAGGGAAAATGCTAT
GGATTACATGCCTTTATCGTACCTATTCGTGAAAATCGGACCCATAAGCCTTTGCCAGGA
ATTACCGTTGGTGACATCGGCCCCAAATTTGGTTATGATGAGATAGACAATGGCTACCTC
AAAATGGACAACCATCGTATTCCCAGAGAAAACATGCTGATGAAGTATGCCCAGGTGAAG
CCTGATGGACCATACGTGAAACCGCTGAGTAACAAGCTGACTTACGGGACCATGGTGTTT
GTCAGGTCCTTCCTTGTGGGAGAAGCTGCTCGGGCTCTGTCTAAGGCGTGCACCATTGCC
ATCCGATACAGCGCTGTGAGGCACCAGTCTGAAATCAAGCCAGGTGAACCAGAACCACAG
ATTTTGGATTTTCAAACCCAGCAGTATAAACTCTTTCCACTCCTGGCCACTGCCTATGCC
TTCCAGTTTGTGGGCGCATACATGAAGGAGACCTATCACCGGATTAACGAAGGCATTGGT
CAAGGGGACCTGAGTGAACTGCCTGAGCTTCATGCCCTCACCGCTGGACTGAAGGCTTTC
ACCTCCTGGACTGCAAACACTGGCATTGAAGCATGTCGGATGGCTTGTGGTGGGCATGGC
TATTCTCATTGCAGTGGTCTTCCAAATATTTATGTCAATTTCACCCCAAGCTGTACCTTT
GAGGGAGAAAACACTGTCATGATGCTCCAGACGGCTAGGTTCCTGATGAAAAGTTATGAT
CAGGTGCACTCAGGAAAGTTGGTGTGTGGCATGGTGTCCTATTTGAACGACCTGCCCAGT
CAGCGCATCCAGCCACAGCAGGTAGCAGTCTGGCCAACCATGGTGGATATCAACAGCCCC
GAAAGCCTAACCGAAGCATATAAACTCCGTGCAGCCAGATTAGTAGAAATTGCTGCAAAA
AACCTTCAAAAAGAAGTGATTCACAGAAAAAGCAAGGAGGTAGCTTGGAACCTAACTTCT
GTTGACCTTGTTCGAGCAAGTGAGGCACATTTGCACTATGGGTTAGTTAAGCTCTTTTCA
GAAAAACTCCTCAAAATTCAAGATAAAGCCATTCAAGCTGTCTTAAGGAGTTTATGTCTG
CTGTATTCTCTGTATGGAATCAGTCAGAACGCGGGGGATTTCCTTCAGGGGAGCATCATG
ACAGAGCCTCAGATTACACAAGTAAACCAGCGTGTAAAGGAGTTACTCACTCTGATTCGC
TCAGATGCTGTTGCTTTGGTTGATGCATTTGATTTTCAGGATGTGACACTTGGCTCTGTG
CTTGGCCGCTATGATGGGAATGTGTATGAAAACTTGTTTGAGTGGGCTAAGAACTCCCCA
CTGAACAAAGCAGAGGTCCACGAATCTTACAAGCACCTGAAGTCACTGCAGTCCAAGCTC
TGA
Enzyme 4 GenBank Gene ID U03268 Link Image
Enzyme 4 GeneCard ID ACOX1 Link Image
Enzyme 4 GenAtlas ID ACOX1 Link Image
Enzyme 4 HGNC ID HGNC:119 Link Image
Enzyme 4 Chromosome Location 17
Enzyme 4 Locus 17q24-q25|17q25.1
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Varanasi U, Chu R, Chu S, Espinosa R, LeBeau MM, Reddy JK: Isolation of the human peroxisomal acyl-CoA oxidase gene: organization, promoter analysis, and chromosomal localization. Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):3107-11. [PubMed Link Image]
  2. Chu R, Varanasi U, Chu S, Lin Y, Usuda N, Rao MS, Reddy JK: Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells. J Biol Chem. 1995 Mar 3;270(9):4908-15. [PubMed Link Image]
  3. Fournier B, Saudubray JM, Benichou B, Lyonnet S, Munnich A, Clevers H, Poll-The BT: Large deletion of the peroxisomal acyl-CoA oxidase gene in pseudoneonatal adrenoleukodystrophy. J Clin Invest. 1994 Aug;94(2):526-31. [PubMed Link Image]
  4. Aoyama T, Tsushima K, Souri M, Kamijo T, Suzuki Y, Shimozawa N, Orii T, Hashimoto T: Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1113-8. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5424
Enzyme 5 Name Acyl-coenzyme A oxidase 3, peroxisomal
Enzyme 5 Synonyms
  1. Pristanoyl-CoA oxidase
  2. Branched-chain acyl-CoA oxidase
  3. BRCACox
Enzyme 5 Gene Name ACOX3
Enzyme 5 Protein Sequence >Acyl-coenzyme A oxidase 3, peroxisomal 
MASTVEGGDTALLPEFPRGPLDAYRARASFSWKELALFTEGEGMLRFKKTIFSALENDPL
FARSPGADLSLEKYRELNFLRCKRIFEYDFLSVEDMFKSPLKVPALIQCLGMYDSSLAAK
YLLHSLVFGSAVYSSGSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPAT
EEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQCHGLHPFIVQIRDPKTLLPMP
GVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGAS
LGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEEEIPVLEYPMQQWRLLPYL
AAVYALDHFSKSLFLDLVELQRGLASGDRSARQAELGREIHALASASKPLASWTTQQGIQ
ECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHDGACFR
SPLKSVDFLDAYPGILDQKFEVSSVADCLDSAVALAAYKWLVCYLLRETYQKLNQEKRSG
SSDFEARNKCQVSHGRPLALAFVELTVVQRFHEHVHQPSVPPSLRAVLGRLSALYALWSL
SRHAALLYRGGYFSGEQAGEVLESAVLALCSQLKDDAVALVDVIAPPDFVLDSPIGRADG
ELYKNLWGAVLQESKVLERASWWPEFSVNKPVIGSLKSKL
Enzyme 5 Number of Residues 700
Enzyme 5 Molecular Weight 77630
Enzyme 5 Theoretical pI 7.27
Enzyme 5 GO Classification
Function
  • FAD binding
  • acyl-CoA dehydrogenase activity
  • acyl-CoA oxidase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
  • purine nucleotide binding
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • electron transport
  • fatty acid beta-oxidation
  • fatty acid metabolism
  • fatty acid oxidation
  • generation of precursor metabolites and energy
  • metabolism
  • organic acid metabolism
  • physiological process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • microbody
  • organelle
  • peroxisome
Enzyme 5 General Function Lipid transport and metabolism
Enzyme 5 Specific Function Oxidizes the CoA-esters of 2-methyl-branched fatty acids
Enzyme 5 Pathways
Enzyme 5 Reactions
  • acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 2326549 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID O15254 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name ACOX3_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2103 bp 
ATGGCATCCACTGTGGAAGGAGGCGACACAGCTCTGCTCCCAGAATTCCCCAGGGGGCCC
CTCGATGCCTACCGAGCAAGAGCGTCCTTCAGCTGGAAGGACGTGGCGCTGTTCACGGAA
GGGGAGGGCAATGTCCGCTTTAAGAAAACCATCTTCTCAGCTCTTGAGAATGACCCTCTT
TTCGCTCGTTCCCCTGGAGCCGACCTGTCCTTGGAGAAGTATCGCGAGCTGAACTTCCTT
CGATGCAAGCGGATCTTCGAGTATGACTTCCTCAGTGTCGAAGCAATGTTCAAGAGCCCT
CTGAAGGTCCCCGCCTTGATTCAGTGCCTGGGCATGTATGACTCTTCTCTGGCTGCCAAG
TACCTCCTCCATAGCTTGGTTTTTGGATCAGCAGTTTACAGTTCTGGTTCTGAAAGACAT
CTCACATATATTCAAAAGATCTTCAGGATGGAGATTTTTGGATGTTTTGCTCTGACCGAA
TTAAGCCACGGCAGTAATACCAAGGCCATTCGCACAACTGCCCACTACGATCCTGCCACT
GAGGAATTCATCATACATTCCCCTGATTTCGAAGCTGCCAAGTTTTGGGTTGGCAACATG
GGCAAGACAGCCACTCACGCGGTGGTGTTTGCTAAGCTGTGTGTGCCAGGGGACCAGTGC
CATGGGCTGCATCCCTTTATCGTGCAGATCCGGGACCCGAAGACCCTTCTTCCCATGCCT
GGAGTGATGGTTGGCGACATAGGAAAAAAACTCGGGCAGAACGGTCTAGATAATGGTTTC
GCCATGTTCCACAAGGTCAGAGTTCCTCGCCAGAGCCTTCTGAACCGGATGGGAGACGTC
ACCCCCGAGGGCACCTATGTCAGCCCCTTTAAGGACGTCAGGCAGCGCTTTGGAGCGTCC
CTGGGGAGCCTGTCCTCGGGCCGGGTCTCCATCGTGAGCCTGGCCATCCTTAACCTAAAG
CTGGCCGTGGCCATCGCTCTTCGCTTCTCAGCCACTCGGCGTCAGTTTGGACCCACAGAG
GAGGAGGAAATACCAGTGCTTGAGTATCCAATGCAGCAATGGCGCTTGCTTCCATATCTG
GCAGCTGTCTACGGCTTAGACCATTTCTCCAAGTCGCTCTTCCTGGACCTGGTGGAGCTC
CAGCGAGGACTTGCATCGGGAGACCGCAGCGCCAGACAGGCAGAGCTTGGACGTGAGATC
CACGCCCTGGCATCGGCCAGCAAGCCCCTGGCCTCGTGGACCACCCAGCAAGGAATTCAG
GAATGCCGGGAGGCGTGTGGAGGACACGGCTATCTGGCCATGAACCGGTTGGGTGTCCTT
AGAGATGACAACGATCCCAACTGCACATACGAAGGTGACAACAACATCCTGCTGCAGCAG
ACAAGCAACTATTTGCTGGGTCTCCTGGCACACCAGGTCCACGATGGAGCTTGCTTCCGC
AGTCCGCTGAAGTCAGTGGACTTTCTGGACGCCTATCCCGGCATCCTTGACCAGAAGTTT
GAGGTCTCCAGTGTTGCCGACTGCTTGGACTCTGCAGTCGCCCTGGCAGCATACAAGTGG
CTGGTTTGCTACCTGCTCCGAGAGACTTATCAAAAATTAAACCAAGAGAAAAGATCAGGA
AGCAGTGACTTTGAAGCAAGGAACAAATGCCAGGTGTCCCACGGCCGTCCGTTGGCGCTG
GCCTTCGTGGAGCTCACGGTGGTCCAGAGGTTCCACGAGCACGTGCACCAGCCTTCCGTG
CCGCCCTCGCTGCGGGCCGTGCTGGGGCGGCTCAGTGCTCTGTACGCCCTGTGGTCCCTG
AAGCGCCACGCGGCCCTGCTCTACCGAGGAGGATACTTCTCCGGTGAGCAGGCGGGAGAA
GTGTTGGAGAGCGCCGTCCTGGCTTTGTGTTCCCAGCTGAAAGACGATGCAGTTGCCCTG
GTAGACGTGATCGCTCCTCCTGACTTTGTTCTGGACTCACCGATTGGCAGAGCCGACGGC
GAGCTCTACAAAAACCTCTGGGGCGCTGTCCTGCAGGAAAGCAAGGTGTTGGAGCGGGCA
TCCTGGTGGCCAGAGTTTTCTGTGAACAAACCTGTCATAGGAAGTCTGAAATCGAAGCTC
TAG
Enzyme 5 GenBank Gene ID Y11411 Link Image
Enzyme 5 GeneCard ID ACOX3 Link Image
Enzyme 5 GenAtlas ID ACOX3 Link Image
Enzyme 5 HGNC ID HGNC:121 Link Image
Enzyme 5 Chromosome Location 4
Enzyme 5 Locus 4p15.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Vanhooren JC, Marynen P, Mannaerts GP, Van Veldhoven PP: Evidence for the existence of a pristanoyl-CoA oxidase gene in man. Biochem J. 1997 Aug 1;325 ( Pt 3):593-9. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6299
Enzyme 6 Name Peroxisomal trans-2-enoyl-CoA reductase
Enzyme 6 Synonyms
  1. TERP
  2. HPDHase
  3. pVI-ARL
  4. 2,4-dienoyl-CoA reductase-related protein
  5. DCR-RP
Enzyme 6 Gene Name PECR
Enzyme 6 Protein Sequence >Peroxisomal trans-2-enoyl-CoA reductase 
MASWAKGRSYLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAAD
ELQANLPPTKQARVIPIQCNIRNEEEVNNLVKSTLDTFGKINFLVNNGGGQFLSPAEHIS
SKGWHAVLETNLTGTFYMCKAVYSSWMKEHGGSIVNIIVPTKAGFPLAVHSGAARAGVYN
LTKSLALEWACSGIRINCVAPGVIYSQTAVENYGSWGQSFFEGSFQKIPAKRIGVPEEVS
SVVCFLLSPAASFITGQSVDVDGGRSLYTHSYEVPDHDNWPKGAGDLSVVKKMKETFKEK
AKL
Enzyme 6 Number of Residues 303
Enzyme 6 Molecular Weight 32545
Enzyme 6 Theoretical pI 9.12
Enzyme 6 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
  • regulation of apoptosis
  • regulation of biological process
  • regulation of cellular physiological process
  • regulation of physiological process
  • regulation of programmed cell death
Component
—
Enzyme 6 General Function Lipid transport and metabolism
Enzyme 6 Specific Function Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions
  • acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 7798698 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9BY49 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PECR_HUMAN Link Image
Enzyme 6 PDB ID 1YXM Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >912 bp 
ATGGCCTCCTGGGCTAAGGGCAGGAGCTACCTGGCGCCTGGTTTGCTGCAGGGCCAAGTG
GCCATCGTCACCGGCGGGGCCACGGGCATCGGAAAAGCCATCGTGAAGGAGCTCCTGGAG
CTGGGGAGTAATGTGGTCATTGCATCCCGTAAGTTGGAGAGATTGAAGTCTGCGGCAGAT
GAACTGCAGGCCAACCTACCTCCCACAAAGCAGGCACGAGTCATTCCCATACAATGCAAC
ATCCGGAATGAGGAGGAGGTGAATAATTTGGTCAAATCTACCTTAGATACTTTTGGTAAG
ATCAATTTCTTGGTGAACAATGGAGGAGGCCAGTTTCTTTCCCCTGCTGAACACATCAGT
TCTAAGGGATGGCACGCTGTGCTTGAGACCAACCTGACGGGTACCTTCTACATGTGCAAA
GCAGTTTACAGCTCCTGGATGAAAGAGCATGGAGGATCTATCGTCAATATCATTGTCCCT
ACTAAAGCTGGATTTCCATTAGCTGTGCATTCTGGAGCTGCAAGAGCAGGTGTTTACAAC
CTCACCAAATCTTTAGCTTTGGAATGGGCCTGCAGTGGAATACGGATCAATTGTGTTGCC
CCTGGAGTTATTTATTCCCAGACTGCTGTGGAGAACTATGGTTCCTGGGGACAAAGCTTC
TTTGAAGGGTCTTTTCAGAAAATCCCCGCTAAACGAATTGGTGTTCCTGAGGAGGTCTCC
TCTGTGGTCTGCTTCCTACTGTCTCCTGCAGCTTCCTTCATCACTGGACAGTCAGTGGAT
GTGGATGGGGGCCGGAGTCTCTATACTCACTCGTATGAGGTACCAGATCATGACAACTGG
CCCAAGGGAGCAGGGGACCTTTCTGTTGTCAAAAAGATGAAGGAGACCTTTAAGGAGAAA
GCTAAGCTCTGA
Enzyme 6 GenBank Gene ID AF232009 Link Image
Enzyme 6 GeneCard ID PECR Link Image
Enzyme 6 GenAtlas ID PECR Link Image
Enzyme 6 HGNC ID HGNC:18281 Link Image
Enzyme 6 Chromosome Location 2
Enzyme 6 Locus 2q35
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Das AK, Uhler MD, Hajra AK: Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs. J Biol Chem. 2000 Aug 11;275(32):24333-40. [PubMed Link Image]
  2. Amery L, Mannaerts GP, Subramani S, Van Veldhoven PP, Fransen M: Identification of a novel human peroxisomal 2,4-dienoyl-CoA reductase related protein using the M13 phage protein VI phage display technology. Comb Chem High Throughput Screen. 2001 Nov;4(7):545-52. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6874
Enzyme 7 Name Glycylpeptide N-tetradecanoyltransferase 1
Enzyme 7 Synonyms
  1. Peptide N- myristoyltransferase 1
  2. Myristoyl-CoA:protein N-myristoyltransferase 1
  3. NMT 1
  4. Type I N-myristoyltransferase
Enzyme 7 Gene Name NMT1
Enzyme 7 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase 1 
MADESETAVKPPAPPLPQMMEGNGNGHEHCSDCENEEDNSYNRGGLSPANDTGAKKKKKK
QKKKKEKGSETDSAQDQPVKMNSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFW
DTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENY
VEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEK
KMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRS
LNPRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMETKDIPVVHQLLTRYLKQF
HLTPVMSQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAY
SFYNVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYN
WKCPSMGAEKVGLVLQ
Enzyme 7 Number of Residues 496
Enzyme 7 Molecular Weight 56807
Enzyme 7 Theoretical pI 7.91
Enzyme 7 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • N-terminal protein myristoylation
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein amino acid myristoylation
  • protein modification
  • protein myristoylation
Component
—
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions
  • tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 3005063 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P30419 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name NMT1_HUMAN Link Image
Enzyme 7 PDB ID 1RXT Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1491 bp 
ATGGCGGACGAGAGTGAGACAGCAGTGAAGCCGCCGGCACCTCCGCTGCCGCAGATGATG
GAAGGGAACGGGAACGGCCATGAGCACTGCAGCGATTGCGAGAATGAGGAGGACAACAGC
TACAACCGGGGTGGTTTGAGTCCAGCCAATGACACTGGAGCCAAAAAGAAGAAAAAGAAA
CAAAAAAAGAAGAAAGAAAAAGGCAGTGAGACAGATTCAGCCCAGGATCAGCCTGTGAAG
ATGAACTCTTTGCCAGCAGAGAGGATCCAGGAAATACAGAAGGCCATTGAGCTGTTCTCA
GTGGGTCAGGGACCTGCCAAAACCATGGAGGAGGCTAGCAAGCGAAGCTACCAGTTCTGG
GATACGCAGCCCGTCCCCAAGCTGGGCGAAGTGGTGAACACCCATGGCCCCGTGGAGCCT
GACAAGGACAATATCCGCCAGGAGCCCTACACCCTGCCCCAGGGCTTCACCTGGGATGCT
TTGGACTTGGGCGATCGTGGTGTGCTAAAAGAACTGTACACCCTCCTGAATGAGAACTAT
GTGGAAGATGATGACAACATGTTCCGATTTGATTATTCCCCGGAGTTTCTTTTGTGGGCT
CTCCGGCCACCCGGCTGGCTCCCCCAGTGGCACTGTGGGGTTCGAGTGGTCTCAAGTCGG
AAATTGGTTGGGTTCATTAGCGCCATCCCAGCAAACATCCATATCTATGACACAGAGAAG
AAGATGGTAGAGATCAACTTCCTGTGTGTCCACAAGAAGCTGCGTTCCAAGAGGGTTGCT
CCAGTTCTGATCCGAGAGATCACCAGGCGGGTTCACCTGGAGGGCATCTTCCAAGCAGTT
TACACTGCCGGGGTGGTACTACCAAAGCCCGTTGGCACCTGCAGGTATTGGCATCGGTCC
CTAAACCCACGGAAGCTGATTGAAGTGAAGTTCTCCCACCTGAGCAGAAATATGACCATG
CAGCGCACCATGAAGCTCTACCGACTGCCAGAGACTCCCAAGACAGCTGGGCTGCGACCA
ATGGAAACAAAGGACATTCCAGTAGTGCACCAGCTCCTCACCAGGTACTTGAAGCAATTT
CACCTTACGCCCGTCATGAGCCAGGAGGAGGTGGAGCACTGGTTCTACCCCCAGGAGAAT
ATCATCGACACTTTCGTGGTGGAGAACGCAAACGGAGAGGTGACAGATTTCCTGAGCTTT
TATACGCTGCCCTCCACCATCATGAACCATCCAACCCACAAGAGTCTCAAAGCTGCTTAT
TCTTTCTACAACGTTCACACCCAGACCCCTCTTCTAGACCTCATGAGCGACGCCCTTGTC
CTCGCCAAAATGAAAGGGTTTGATGTGTTCAATGCACTGGATCTCATGGAGAACAAAACC
TTCCTGGAGAAGCTCAAGTTTGGCATAGGGGACGGCAACCTGCAGTATTACCTTTACAAT
TGGAAATGCCCCAGCATGGGGGCAGAGAAGGTTGGACTGGTGCTACAATAA
Enzyme 7 GenBank Gene ID AF043324 Link Image
Enzyme 7 GeneCard ID NMT1 Link Image
Enzyme 7 GenAtlas ID NMT1 Link Image
Enzyme 7 HGNC ID HGNC:7857 Link Image
Enzyme 7 Chromosome Location 17
Enzyme 7 Locus 17q21.31
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Glover CJ, Hartman KD, Felsted RL: Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction. J Biol Chem. 1997 Nov 7;272(45):28680-9. [PubMed Link Image]
  2. Giang DK, Cravatt BF: A second mammalian N-myristoyltransferase. J Biol Chem. 1998 Mar 20;273(12):6595-8. [PubMed Link Image]
  3. Duronio RJ, Reed SI, Gordon JI: Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1992 May 1;89(9):4129-33. [PubMed Link Image]
  4. McIlhinney RA, Young K, Egerton M, Camble R, White A, Soloviev M: Characterization of human and rat brain myristoyl-CoA:protein N-myristoyltransferase: evidence for an alternative splice variant of the enzyme. Biochem J. 1998 Aug 1;333 ( Pt 3):491-5. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6876
Enzyme 8 Name Glycylpeptide N-tetradecanoyltransferase 2
Enzyme 8 Synonyms
  1. Peptide N- myristoyltransferase 2
  2. Myristoyl-CoA:protein N-myristoyltransferase 2
  3. NMT 2
  4. Type II N-myristoyltransferase
Enzyme 8 Gene Name NMT2
Enzyme 8 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase 2 
MAEDSESAASQQSLELDDQDTCGIDGDNEEETEHAKGSPGGYLGAKKKKKKQKRKKEKPN
SGGTKSDSASDSQEIKIQQPSKNPSVPMQKLQDIQRAMELLSACQGPARNIDEAAKHRYQ
FWDTQPVPKLDEVITSHGAIEPDKDNVRQEPYSLPQGFMWDTLDLSDAEVLKELYTLLNE
NYVEDDDNMFRFDYSPEFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDS
VKKMVEINFLCVHKKLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPIATCRYWH
RSLNPRKLVEVKFSHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIKSVRELINTYLK
QFHLAPVMDEEEVAHWFLPREHIIDTFVVESPNGKLTDFLSFYTLPSTVMHHPAHKSLKA
AYSFYNIHTETPLLDLMSDALILAKSKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYL
YNWRCPGTDSEKVGLVLQ
Enzyme 8 Number of Residues 498
Enzyme 8 Molecular Weight 56981
Enzyme 8 Theoretical pI 7.65
Enzyme 8 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • N-terminal protein myristoylation
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein amino acid myristoylation
  • protein modification
  • protein myristoylation
Component
—
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 3005065 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID O60551 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name NMT2_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1497 bp 
ATGGCGGAGGACAGCGAGTCTGCGGCCAGCCAGCAGAGCCTGGAACTGGACGACCAGGAC
ACGTGCGGGATAGACGGGGACAATGAGGAGGAGACGGAGCACGCCAAAGGAAGTCCTGGA
GGGTATTTGGGAGCCAAAAAGAAAAAGAAGAAACAGAAGAGAAAAAAGGAGAAACCAAAT
TCCGGAGGCACCAAGTCAGACTCGGCATCTGATTCCCAGGAGATTAAAATTCAGCAGCCT
TCGAAAAATCCCAGTGTTCCAATGCAGAAGTTGCAGGATATCCAGAGAGCAATGGAGCTG
CTATCCGCATGCCAGGGCCCAGCCAGGAACATTGATGAGGCTGCAAAGCACAGATACCAG
TTTTGGGACACACAACCGGTACCAAAACTAGATGAAGTCATAACATCTCATGGTGCAATT
GAACCAGATAAAGACAACGTACGCCAAGAACCGTATTCTTTGCCACAGGGTTTTATGTGG
GACACTTTAGACTTGAGTGATGCCGAAGTGCTCAAGGAGTTATACACGTTGTTAAATGAG
AATTACGTAGAAGATGATGACAATATGTTCCGATTTGACTATTCACCCGAGTTCCTGTTG
TGGGCTCTGCGTCCACCAGGCTGGCTCCTGCAGTGGCACTGTGGGGTCAGAGTGTCTTCA
AATAAAAAACTGGTCGGGTTCATAAGTGCCATCCCAGCAAACATTCGGATTTATGACAGT
GTGAAGAAGATGGTAGAAATCAACTTTCTTTGTGTTCATAAGAAGTTGAGATCGAAACGG
GTAGCCCCAGTGCTAATCCGAGAGATCACTAGAAGAGTGAACCTGGAAGGGATCTTCCAG
GCTGTGTACACCGCGGGAGTGGTTCTTCCTAAGCCCATAGCCACATGCAGATACTGGCAT
CGATCACTAAACCCCAGAAAATTGGTAGAAGTGAAATTTTCTCACTTGAGTAGAAATATG
ACTTTACAGAGAACAATGAAGCTATACAGACTTCCAGATGTTACAAAGACTTCAGGTTTG
AGACCAATGGAACCAAAAGATATCAAATCAGTTCGAGAATTAATCAACACTTACCTGAAG
CAGTTTCATCTGGCTCCAGTGATGGATGAAGAGGAAGTAGCCCACTGGTTCCTCCCCCGG
GAGCACATTATTGACACGTTTGTAGTGGAGAGCCCCAACGGTAAACTGACTGATTTCCTG
AGCTTCTATACGCTCCCCTCCACGGTGATGCACCACCCTGCTCACAAGAGCCTCAAAGCC
GCCTACTCATTCTACAACATCCACACAGAGACGCCCCTGCTGGACCTCATGAGCGACGCG
CTCATCCTGGCTAAATCGAAAGGATTTGATGTATTCAATGCACTGGATTTGATGGAAAAT
AAGACATTCTTGGAAAAACTCAAGTTTGGTATAGGAGATGGCAATTTGCAGTATTACCTG
TACAATTGGAGGTGTCCAGGTACAGATTCTGAAAAGGTTGGACTAGTACTACAATAG
Enzyme 8 GenBank Gene ID AF043325 Link Image
Enzyme 8 GeneCard ID NMT2 Link Image
Enzyme 8 GenAtlas ID NMT2 Link Image
Enzyme 8 HGNC ID HGNC:7858 Link Image
Enzyme 8 Chromosome Location 10
Enzyme 8 Locus 10p13
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Giang DK, Cravatt BF: A second mammalian N-myristoyltransferase. J Biol Chem. 1998 Mar 20;273(12):6595-8. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 13023
Enzyme 9 Name Acyl-Coenzyme A dehydrogenase, long chain
Enzyme 9 Synonyms
  1. Putative uncharacterized protein ACADL
Enzyme 9 Gene Name ACADL
Enzyme 9 Protein Sequence >Acyl-Coenzyme A dehydrogenase, long chain 
MAARLLRGSLRVLGGHRAPRQLPAARCSHSGGEERLETPSAKKLTDIGIRRIFSPEHDIF
RKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIV
WEEQAYSNCSGPGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSD
LQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVIVVAVTNHEAPSPAHGISLFLVENGMK
GFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLLIADVAI
SASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRL
DSATACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKE
LIAREIVFDK
Enzyme 9 Number of Residues 430
Enzyme 9 Molecular Weight 47656
Enzyme 9 Theoretical pI 7.89
Enzyme 9 GO Classification
Function
  • acyl-CoA dehydrogenase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 9 General Function Lipid transport and metabolism
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 24660234 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q8IUN8 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name Q8IUN8_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID BC039063 Link Image
Enzyme 9 GeneCard ID Q8IUN8 Link Image
Enzyme 9 GenAtlas ID ACADL Link Image
Enzyme 9 HGNC ID HGNC:88 Link Image
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 15876
Enzyme 10 Name ACAA1 protein
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name Not Available
Enzyme 10 Protein Sequence >ACAA1 protein 
MQRLQVVLGHLRGPADSGWMPQAAPCLSGAPQASAADVVVVHGRRTAICRAGRGGFKDTT
PDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPETVPLSTVN
RQCSSGLQAVASIAGGIRNGSYDIGMACGITSENVAERFGISREKQDTFALASQQKAARA
QSKGCFQAEIVPVTTTVHDDKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAG
LTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGARQAITLLNE
LKRRGKRAYGVVSMCIGTGMGAAAVFEYPGN
Enzyme 10 Number of Residues 331
Enzyme 10 Molecular Weight 34637
Enzyme 10 Theoretical pI 8.49
Enzyme 10 GO Classification Not Available
Enzyme 10 General Function Lipid transport and metabolism
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein Not Available
Enzyme 10 UniProtKB/Swiss-Prot ID Q96CA6 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name Q96CA6_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID BC014474 Link Image
Enzyme 10 GeneCard ID Q96CA6 Link Image
Enzyme 10 GenAtlas ID ACAA1 Link Image
Enzyme 10 HGNC ID HGNC:82 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs Not Available
Enzyme 10 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 16031
Enzyme 11 Name cDNA FLJ76905, highly similar to Homo sapiens N-myristoyltransferase 1 (NMT1), mRNA (N-myristoyltransferase 1, isoform CRA_b)
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name NMT1
Enzyme 11 Protein Sequence >cDNA FLJ76905, highly similar to Homo sapiens N-myristoyltransferase 1 (NMT1), mRNA (N-myristoyltransferase 1, isoform CRA_b) 
MADESETAVKPPAPPLPQMMEGNGNGHEHCSDCENEEDNSYNRGGLSPANDTGAKKKKKK
QKKKKEKGSETDSAQDQPVKMNSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFW
DTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENY
VEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEK
KMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRS
LNPRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMETKDIPVVHQLLTRYLKQF
HLTPVMSQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAY
SFYNVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYN
WKCPSMGAEKVGLVLQ
Enzyme 11 Number of Residues 496
Enzyme 11 Molecular Weight 56807
Enzyme 11 Theoretical pI 7.91
Enzyme 11 GO Classification Not Available
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function Not Available
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein Not Available
Enzyme 11 UniProtKB/Swiss-Prot ID A8K7C1 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name A8K7C1_HUMAN Link Image
Enzyme 11 PDB ID 1RXT Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID AK291936 Link Image
Enzyme 11 GeneCard ID A8K7C1 Link Image
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location 17
Enzyme 11 Locus 17q21.31
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References Not Available
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 16712
Enzyme 12 Name cDNA FLJ30111 fis, clone BNGH42000360, highly similar to 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16)
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name Not Available
Enzyme 12 Protein Sequence >cDNA FLJ30111 fis, clone BNGH42000360, highly similar to 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16) 
MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVL
QSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTE
SMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECD
KYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFK
KDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAI
SGALKKAGLSLKDMDLVEANEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSR
ITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA
Enzyme 12 Number of Residues 397
Enzyme 12 Molecular Weight 41897
Enzyme 12 Theoretical pI 8.21
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Lipid transport and metabolism
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions
  • acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA [RN:R00391] ALL_REAC R00391 > R00238 R00829 R00927 R01177 R03778 R03858 R03991 R04742 R04747 R05506 R07937 R07953
  • (other) R03719 R04546 R04811
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID B3KNP8 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name B3KNP8_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID AK054673 Link Image
Enzyme 12 GeneCard ID B3KNP8 Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs Not Available
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 16766
Enzyme 13 Name Glycylpeptide N-tetradecanoyltransferase
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name NMT2
Enzyme 13 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase 
MAEDSESAASQQSLELDDQDTCGIDGDNEEETEHAKGSPGGYLGAKKKKKKQKRKKEKPN
SGGTKSDSASDSQEIKIQQPSKNPSVPMQKLQDIQRAMELLSACQGPARNIDEAAKHRYQ
FWDTQPVPKLDEVITSHGAIEPDKDNVRQEPYSLPQGFMWDTLDLSDAEVLKELYTLLNE
NYVEDDDNMFRFDYSPEFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDS
VKKMVEINFLCVHKKLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPIATCRYWH
RSLNPRKLVEVKFSHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIKSVRELINTYLK
QFHLAPVMDEEEVAHWFLPREHIIDTFVVESPNGKLTDFLSFYTLPSTVMHHPAHKSLKA
AYSFYNIHTETPLLDLMSDALILAKSKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYL
YNWRCPGTDSEKVGLVLQ
Enzyme 13 Number of Residues 498
Enzyme 13 Molecular Weight 56981
Enzyme 13 Theoretical pI 7.65
Enzyme 13 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • N-terminal protein myristoylation
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein amino acid myristoylation
  • protein modification
  • protein myristoylation
Component
—
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein Not Available
Enzyme 13 UniProtKB/Swiss-Prot ID B0YJ49 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name B0YJ49_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence Not Available
Enzyme 13 GenBank Gene ID EF445001 Link Image
Enzyme 13 GeneCard ID B0YJ49 Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location 10
Enzyme 13 Locus 10p13
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 16884
Enzyme 14 Name Glycylpeptide N-tetradecanoyltransferase
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name NMT2
Enzyme 14 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase 
KKRRSLPAEVLEGIWEPKRKRRNRREKRRNQIPEAPSQTRHLIPRRLKFSSLRNTTPSGS
RFQREQPWNPSVPMQKLQDIQRAMELLSACQGPARNIDEAAKHRYQFWDTQPVPKLDEVI
TSHGAIEPDKDNVRQEPYSLPQGFMWDTLDLSDAEVLKELYTLLNENYVEDDDNMFRFDY
SPEFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKKMVEINFLCVHK
KLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPIATCRYWHRSLNPRKLVEVKFS
HLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIKSVRELINTYLKQFHLAPVMDEEEVA
HWFLPREHIIDTFVVESPNGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPLL
DLMSDALILAKSKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTDSEKVG
LVLQ
Enzyme 14 Number of Residues 484
Enzyme 14 Molecular Weight 56485
Enzyme 14 Theoretical pI 9.96
Enzyme 14 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • N-terminal protein myristoylation
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein amino acid myristoylation
  • protein modification
  • protein myristoylation
Component
—
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein Not Available
Enzyme 14 UniProtKB/Swiss-Prot ID A8MWH3 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name A8MWH3_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence Not Available
Enzyme 14 GenBank Gene ID AL590365 Link Image
Enzyme 14 GeneCard ID A8MWH3 Link Image
Enzyme 14 GenAtlas ID NMT2 Link Image
Enzyme 14 HGNC ID HGNC:7858 Link Image
Enzyme 14 Chromosome Location 10
Enzyme 14 Locus 10p13
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References Not Available
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 16885
Enzyme 15 Name Glycylpeptide N-tetradecanoyltransferase
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name NMT1
Enzyme 15 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase 
DESETAVKPPAPPLPQMMEGNGNGHEHCSDCENEEDNSYNRGGLSPANDTGAKKKKKKQK
KKKEKGSETDSAQDQPVKMNSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFWDT
QPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENYVE
DDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEKKM
VEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLN
PRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMETKDIPVVHQLLTRYLKQFHL
TPVMSQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAYSF
YNVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWK
CPSMGAEKVGLVLQ
Enzyme 15 Number of Residues 494
Enzyme 15 Molecular Weight 56605
Enzyme 15 Theoretical pI 7.91
Enzyme 15 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • N-terminal protein myristoylation
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein amino acid myristoylation
  • protein modification
  • protein myristoylation
Component
—
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID Q96HI4 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name Q96HI4_HUMAN Link Image
Enzyme 15 PDB ID 1RXT Link Image
Enzyme 15 PDB File Show
Enzyme 15 3D Structure
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence Not Available
Enzyme 15 GenBank Gene ID BC008579 Link Image
Enzyme 15 GeneCard ID Q96HI4 Link Image
Enzyme 15 GenAtlas ID NMT1 Link Image
Enzyme 15 HGNC ID HGNC:7857 Link Image
Enzyme 15 Chromosome Location 17
Enzyme 15 Locus 17q21.31
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References Not Available
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 16886
Enzyme 16 Name Glycylpeptide N-tetradecanoyltransferase
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name NMT2
Enzyme 16 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase 
MAEDSESAASQQSLELDDQDTCGIDGDNEEETEHAKGSPGGYLGAKKKKKKQKRKKEKPN
SGGTKSDSASDSQEIKIQQPSKHNTIWQQISAGAAMGSATMEGEWTGMRNDHRNPSVPMQ
KLQDIQRAMELLSACQGPARNIDEAAKHRYQFWDTQPVPKLDEVITSHGAIEPDKDNVRQ
EPYSLPQGFMWDTLDLSDAEVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWL
LQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKKMVEINFLCVHKKLRSKRVAPVLIREI
TRRVNLEGIFQAVYTAGVVLPKPIATCRYWHRSLNPRKLVEVKFSHLSRNMTLQRTMKLY
RLPDVTKTSGLRPMEPKDIKSVRELINTYLKQFHLAPVMDEEEVAHWFLPREHIIDTFVV
ESPNGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPLLDLMSDALILAKSKGF
DVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTDSEKVRLVLN
Enzyme 16 Number of Residues 529
Enzyme 16 Molecular Weight 60493
Enzyme 16 Theoretical pI 7.68
Enzyme 16 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • N-terminal protein myristoylation
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein amino acid myristoylation
  • protein modification
  • protein myristoylation
Component
—
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein Not Available
Enzyme 16 UniProtKB/Swiss-Prot ID A8MWF5 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name A8MWF5_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence Not Available
Enzyme 16 GenBank Gene ID AL590365 Link Image
Enzyme 16 GeneCard ID A8MWF5 Link Image
Enzyme 16 GenAtlas ID NMT2 Link Image
Enzyme 16 HGNC ID HGNC:7858 Link Image
Enzyme 16 Chromosome Location 10
Enzyme 16 Locus 10p13
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References Not Available
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 16887
Enzyme 17 Name Glycylpeptide N-tetradecanoyltransferase
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name NMT2
Enzyme 17 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase 
MAEDSESAASQQSLELDDQDTCGIDGDNEEETEHAKGSPGGYLGAKKKKKKQKRKKEKPN
SGGTKSDSASDSQEIKIQQPSKHNTIWQQISAGAAMGSATMEGEWTGMRNDHKNPSVPMQ
KLQDIQRAMELLSACQGPARNIDEAAKHRYQFWDTQPVPKLDEVITSHGAIEPDKDNVRQ
EPYSLPQGFMWDTLDLSDAEVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWL
LQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKKMVEINFLCVHKKLRSKRVAPVLIREI
TRRVNLEGIFQAVYTAGVVLPKPIATCRYWHRSLNPRKLVEVKFSHLSRNMTLQRTMKLY
RLPDVTKTSGLRPMEPKDIKSVRELINTYLKQFHLAPVMDEEEVAHWFLPREHIIDTFVV
ESPNGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPLLDLMSDALILAKSKGF
DVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTDSEKVGLVLQ
Enzyme 17 Number of Residues 529
Enzyme 17 Molecular Weight 60380
Enzyme 17 Theoretical pI 7.46
Enzyme 17 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • N-terminal protein myristoylation
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein amino acid myristoylation
  • protein modification
  • protein myristoylation
Component
—
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein Not Available
Enzyme 17 UniProtKB/Swiss-Prot ID Q5VUC7 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name Q5VUC7_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence Not Available
Enzyme 17 GenBank Gene ID EF445001 Link Image
Enzyme 17 GeneCard ID Q5VUC7 Link Image
Enzyme 17 GenAtlas ID Not Available
Enzyme 17 HGNC ID Not Available
Enzyme 17 Chromosome Location 10
Enzyme 17 Locus 10p13
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References Not Available
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 16888
Enzyme 18 Name Glycylpeptide N-tetradecanoyltransferase
Enzyme 18 Synonyms Not Available
Enzyme 18 Gene Name NMT2
Enzyme 18 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase 
MRRRRSTPKEVLEGIWEPKRKRRNRREKRRNQIPEAPSQTRHLIPRRLKFSSLRNTTPSG
SRFQREQPWNPSVPMQKLQDIQRAMELLSACQGPARNIDEAAKHRYQFWDTQPVPKLDEV
ITSHGAIEPDKDNVRQEPYSLPQGFMWDTLDLSDAEVLKELYTLLNENYVEDDDNMFRFD
YSPEFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKKMVEINFLCVH
KKLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPIATCRYWHRSLNPRKLVEVKF
SHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIKSVRELINTYLKQFHLAPVMDEEEV
AHWFLPREHIIDTFVVESPNGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPL
LDLMSDALILAKSKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTDSEKV
GLVLQ
Enzyme 18 Number of Residues 485
Enzyme 18 Molecular Weight 56717
Enzyme 18 Theoretical pI 10.02
Enzyme 18 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • N-terminal protein myristoylation
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein amino acid myristoylation
  • protein modification
  • protein myristoylation
Component
—
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein Not Available
Enzyme 18 UniProtKB/Swiss-Prot ID Q5VUC6 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name Q5VUC6_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence Not Available
Enzyme 18 GenBank Gene ID EF445001 Link Image
Enzyme 18 GeneCard ID Q5VUC6 Link Image
Enzyme 18 GenAtlas ID Not Available
Enzyme 18 HGNC ID Not Available
Enzyme 18 Chromosome Location 10
Enzyme 18 Locus 10p13
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References Not Available
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 16889
Enzyme 19 Name Glycylpeptide N-tetradecanoyltransferase
Enzyme 19 Synonyms Not Available
Enzyme 19 Gene Name NMT1
Enzyme 19 Protein Sequence >Glycylpeptide N-tetradecanoyltransferase 
YWAGLRPMETKDIPVVHQLLTRYLKQFHLTPVMSQEEVEHWFYPQENIIDTFVVENANGE
VTDFLSFYTLPSTIMNHPTHKSLKAAYSFYNVHTQTPLLDLMSDALVLAKMVRSRRGGLW
RCAGKGQWSHGEHSSRDAASHGLEALSPPHLFCLGRVPAVFRQKLKTWREQGASEVKALN
SS
Enzyme 19 Number of Residues 182
Enzyme 19 Molecular Weight 20764
Enzyme 19 Theoretical pI 8.69
Enzyme 19 GO Classification
Function
  • N-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • glycylpeptide N-tetradecanoyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring groups other than amino-acyl groups
Process
  • N-terminal protein myristoylation
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid lipidation
  • protein amino acid myristoylation
  • protein modification
  • protein myristoylation
Component
—
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein Not Available
Enzyme 19 UniProtKB/Swiss-Prot ID A4FU65 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name A4FU65_HUMAN Link Image
Enzyme 19 PDB ID 1RXT Link Image
Enzyme 19 PDB File Show
Enzyme 19 3D Structure
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence Not Available
Enzyme 19 GenBank Gene ID BC109226 Link Image
Enzyme 19 GeneCard ID A4FU65 Link Image
Enzyme 19 GenAtlas ID Not Available
Enzyme 19 HGNC ID Not Available
Enzyme 19 Chromosome Location 17
Enzyme 19 Locus 17q21.31
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References Not Available
Enzyme 19 Metabolite References Not Available