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Human Metabolome Database Version 2.5

 

Showing metabocard for 3-Oxohexadecanoyl-CoA (HMDB06402)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2007-05-23 06:35:22
Update Date 2009-06-23 13:44:49
Accession Number HMDB06402
Secondary Accession Numbers Not Available
Common Name 3-Oxohexadecanoyl-CoA
Description 3-Oxohexadecanoyl-CoA has a role in the synthesis and oxidation of fatty acid. It is involved in the pathway, fatty acid elongation in mitochondria. In this pathway Acetyl-CoA is acted upon by the enzyme, acetyl-CoA C-acyltransferase to produce 3-Oxohexadecanoyl-CoA. Since coenzyme A is chemically a thiol, it can react with carboxylic acids to form thioesters, thus functioning as an acyl group carrier. It assists in transferring fatty acids from the cytoplasm to the mitochondria. A molecule of coenzyme A carrying an acetyl group is also referred to as acetyl-CoA. When it is not attached to an acyl group it is usually referred to as 'CoASH' or 'HSCoA'.
Synonyms
  1. 3-Ketopalmitoyl-CoA
  2. 3-Oxopalmitoyl-CoA
  3. 3-Ketopalmitoyl-Coenzyme A
  4. 3-Oxopalmitoyl-Coenzyme A;3-oxopalmitoleoyl-CoA
  5. 3-ketopalmitoleoyl-CoA
  6. 3-oxo-cis-9-hexadecenoyl-CoA
  7. 3-oxohexadec-9Z-enoyl-CoA
  8. 3-oxohexadec-cis-9-enoyl-CoA
Chemical IUPAC Name [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-2-[[hydroxy-[hydroxy-[3-hydroxy-2,2-dimethyl-3-[2-[2-(3-oxohexadecanoylsulfanyl)ethylcarbamoyl]ethylcarbamoyl]propoxy]phosphoryl]oxy-phosphoryl]oxymethyl]oxolan-3-yl]oxyphosphonic acid
Chemical Formula C37H64N7O18P3S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Coenzyme A Derivatives
Sub Class
  • Long chain acyl CoAs
Family
  • Mammalian Metabolite
Species
  • ketone
  • 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 1019.926
Monoisotopic Molecular Weight 1019.324158
Isomeric SMILES CCCCCCCCCCCCCC(=O)CC(=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=C(N)N=CN=C12
Canonical SMILES CCCCCCCCCCCCCC(=O)CC(=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=C(N)N=CN=C12
KEGG Compound ID C05259 Link Image
BioCyc ID 3-OXOPALMITOYL-COA Link Image
BiGG ID 45445 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB06402 Link Image
Metagene Link HMDB06402 Link Image
METLIN ID Not Available
PubChem Compound 440601 Link Image
PubChem Substance 7646 Link Image
ChEBI ID 15491 Link Image
CAS Registry Number 34619-89-1
InChI Identifier InChI=1/C37H64N7O18P3S/c1-4-5-6-7-8-9-10-11-12-13-14-15-25(45)20-28(47)66-19-18-39-27(46)16-17-40-35(50)32(49)37(2,3)22-59-65(56,57)62-64(54,55)58-21-26-31(61-63(51,52)53)30(48)36(60-26)44-24-43-29-33(38)41-23-42-34(29)44/h23-24,26,30-32,36,48-49H,4-22H2,1-3H3,(H,39,46)(H,40,50)(H,54,55)(H,56,57)(H2,38,41,42)(H2,51,52,53)/t26-,30-,31-,32?,36-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.01 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.8 [Predicted by PubChem via XLOGP]; 1.96 [Predicted by ALOGPS] 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 Not Available
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
  • peroxisome
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Fatty Acid Elongation In Mitochondria SMP00054 Link Image map00062 Link Image
Fatty acid Metabolism SMP00051 Link Image map00071 Link Image
General References Not Available
Metabolic Enzymes
  1. 3-ketoacyl-CoA thiolase, mitochondrial
  2. 3-ketoacyl-CoA thiolase, peroxisomal precursor
  3. Trifunctional enzyme subunit beta, mitochondrial precursor
  4. 3-hydroxyacyl-CoA dehydrogenase type-2
  5. Peroxisomal bifunctional enzyme
  6. Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial precursor
  7. Trifunctional enzyme subunit alpha, mitochondrial precursor
  8. Peroxisomal multifunctional enzyme type 2
  9. Hydroxyacyl-Coenzyme A dehydrogenase, type II
  10. Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase
  11. Putative uncharacterized protein
  12. Estradiol 17-beta-dehydrogenase 12
  13. ACAA1 protein
  14. cDNA FLJ30111 fis, clone BNGH42000360, highly similar to 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16)
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 5274
Enzyme 2 Name 3-ketoacyl-CoA thiolase, peroxisomal precursor
Enzyme 2 Synonyms
  1. Beta- ketothiolase
  2. Acetyl-CoA acyltransferase
  3. Peroxisomal 3-oxoacyl-CoA thiolase
Enzyme 2 Gene Name ACAA1
Enzyme 2 Protein Sequence >3-ketoacyl-CoA thiolase, peroxisomal precursor 
MQRLQVVLGHLRGPADSGWMPQAAPCLSGAPQASAADVVVVHGRRTAICRAGRGGFKDTT
PDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPETVPLSTVN
RQCSSGLQAVASIAGGIRNGSYDIGMACGVESMSLADRGNPGNITSRLMEKEKARDCLIP
MGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPVTTTVHDDKGTKRSI
TVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPI
LGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLR
LPPEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRAYGVVSMCIGTGMGAAAVFE
YPGN
Enzyme 2 Number of Residues 424
Enzyme 2 Molecular Weight 44293
Enzyme 2 Theoretical pI 8.55
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 23874 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P09110 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name THIK_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1275 bp 
ATGCAGAGGCTGCAGGTAGTGCTGGGCCACCTGAGGGGTCCGGCCGATTCCGGCTGGATG
CCGCAGGCCGCGCCTTGCCTGAGCGGTGCCCCGCAGGCCTCGGCCGCGGACGTGGTGGTG
GTGCACGGGCGGCGCACGGCCATCTGCCGGGCGGGCCGCGGCGGCTTCAAGGACACCACC
CCCGACGAGCTTCTCTCGGCAGTCATGACCGCGGTTCTCAAGGACGTGAATCTGAGGCCG
GAACAGCTGGGGGACATCTGTGTCGGAAATGTGCTGCAGCCTGGGGCCGGGGCAATCATG
GCCCGAATCGCCCAGTTTCTGAGTGACATCCCGGAGACTGTGCCTTTGTCCACTGTCAAT
AGACAGTGCTCGTCGGGGCTACAGGCAGTGGCCAGCATAGCAGGTGGCATCAGAAATGGG
TCTTATGACATTGGCATGGCCTGTGGGGTGGAGTCCATGTCCCTGGCTGACAGAGGGAAC
CCTGGAAATATTACTTCGCGCTTGATGGAGAAGGAGAAGGCCAGAGATTGCCTGATTCCT
ATGGGGATAACCTCTGAGAATGTGGCTGAGCGGTTTGGCATTTCACGGGAGAAGCAGGAT
ACCTTTGCCCTGGCTTCCCAGCAGAAGGCAGCAAGAGCCCAGAGCAAGGGCTGTTTCCAA
GCTGAGATTGTGCCTGTGACCACCACGGTCCATGATGACAAGGGCACCAAGAGGAGCATC
ACTGTGACCCAGGATGAGGGTATCCGCCCCAGCACCACCATGGAGGGCCTGGCCAAACTG
AAGCCTGCCTTCAAGAAAGATGGTTCTACCACAGCTGGAAACTCTAGCCAGGTGAGTGAT
GGGGCAGCTGCCATCCTGCTGGCCCGGAGGTCCAAGGCAGAAGAGTTGGGCCTTCCCATC
CTTGGGGTCCTGAGGTCTTATGCAGTGGTTGGGGTCCCACCTGACATCATGGGCATTGGA
CCTGCCTATGCCATCCCAGTAGCTTTGCAAAAAGCAGGGCTGACAGTGAGTGACGTGGAC
ATCTTCGAGATCAATGAGGCCTTTGCAAGCCAGGCTGCCTACTGTGTGGAGAAGCTACGA
CTCCCCCCTGAGAAGGTGAACCCCCTGGGGGGTGCAGTGGCCTTAGGGCACCCACTGGGC
TGCACTGGGGCACGACAGGTCATCACGCTGCTCAATGAGCTGAAGCGCCGTGGGAAGAGG
GCATACGGAGTGGTGTCCATGTGCATCGGGACTGGAATGGGAGCCGCTGCCGTCTTTGAA
TACCCTGGGAACTGA
Enzyme 2 GenBank Gene ID X12966 Link Image
Enzyme 2 GeneCard ID ACAA1 Link Image
Enzyme 2 GenAtlas ID ACAA1 Link Image
Enzyme 2 HGNC ID HGNC:82 Link Image
Enzyme 2 Chromosome Location 3
Enzyme 2 Locus 3p23-p22
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Bout A, Teunissen Y, Hashimoto T, Benne R, Tager JM: Nucleotide sequence of human peroxisomal 3-oxoacyl-CoA thiolase. Nucleic Acids Res. 1988 Nov 11;16(21):10369. [PubMed Link Image]
  2. Fairbairn LJ, Tanner MJ: Complete cDNA sequence of human foetal liver peroxisomal 3-oxoacyl-CoA thiolase. Nucleic Acids Res. 1989 May 11;17(9):3588. [PubMed Link Image]
  3. Bout A, Franse MM, Collins J, Blonden L, Tager JM, Benne R: Characterization of the gene encoding human peroxisomal 3-oxoacyl-CoA thiolase (ACAA). No large DNA rearrangement in a thiolase-deficient patient. Biochim Biophys Acta. 1991 Aug 27;1090(1):43-51. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5277
Enzyme 3 Name Trifunctional enzyme subunit beta, mitochondrial precursor
Enzyme 3 Synonyms
  1. TP-beta[Includes: 3-ketoacyl-CoA thiolase
  2. Acetyl-CoA acyltransferase
  3. Beta-ketothiolase]
Enzyme 3 Gene Name HADHB
Enzyme 3 Protein Sequence >Trifunctional enzyme subunit beta, mitochondrial precursor 
MTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAPAVQTKTKKTLAKPNIRNVVVVDGV
RTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAA
LGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMR
KLMLDLNKAKSMGQRLSLISKFRFNFLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLE
QDEYALRSHSLAKKAQDEGLLSDVVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPY
GTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATP
KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNW
GGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYPK
Enzyme 3 Number of Residues 474
Enzyme 3 Molecular Weight 51295
Enzyme 3 Theoretical pI 9.94
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Enzyme 3 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 3 Reactions
  • acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 862458 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P55084 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ECHB_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 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 3 GenBank Gene ID D16481 Link Image
Enzyme 3 GeneCard ID HADHB Link Image
Enzyme 3 GenAtlas ID HADHB Link Image
Enzyme 3 HGNC ID HGNC:4803 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 2p23
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5616
Enzyme 4 Name 3-hydroxyacyl-CoA dehydrogenase type-2
Enzyme 4 Synonyms
  1. 3-hydroxyacyl- CoA dehydrogenase type II
  2. Type II HADH
  3. 3-hydroxy-2-methylbutyryl- CoA dehydrogenase
  4. Endoplasmic reticulum-associated amyloid beta-peptide-binding protein
  5. Short-chain type dehydrogenase/reductase XH98G2
Enzyme 4 Gene Name HSD17B10
Enzyme 4 Protein Sequence >3-hydroxyacyl-CoA dehydrogenase type-2 
MAAACRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVF
APADVTSEKDVQTALALAKGKFGRVDVAVNCAGIAVASKTYNLKKGQTHTLEDFQRVLDV
NLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTL
PIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAI
IENPFLNGEVIRLDGAIRMQP
Enzyme 4 Number of Residues 261
Enzyme 4 Molecular Weight 26923
Enzyme 4 Theoretical pI 7.94
Enzyme 4 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 4 General Function Lipid transport and metabolism
Enzyme 4 Specific Function Binds intracellular amyloid-beta. By interacting with amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD)
Enzyme 4 Pathways
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 4 Reactions
  • (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ = 2-methylacetoacetyl-CoA + NADH + H+
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-27
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 2558754 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q99714 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name HCD2_HUMAN Link Image
Enzyme 4 PDB ID 1SO8 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >786 bp 
ATGGCAGCAGCGTGTCGGAGCGTGAAGGGCCTGGTGGCGGTAATAACCGGAGGAGCCTCG
GGCCTGGGCCTGGCCACGGCGGAGCGACTTGTGGGGCAGGGAGCCTCTGCTGTGCTTCTG
GACCTGCCCAACTCGGGTGGGGAGGCCCAAGCCAAGAAGTTAGGAAACAACTGCGTTTTC
GCCCCAGCCGACGTGACCTCTGAGAAGGATGTGCAAACAGCTCTGGCTCTAGCAAAAGGA
AAGTTTGGCCGTGTGGATGTAGCTGTCAACTGTGCAGGCATCGCGGTGGCTAGCAAGACG
TACAACTTAAAGAAGGGCCAGACCCATACCTTGGAAGACTTCCAGCGAGTTCTTGATGTG
AATCTCATGGGCACCTTCAATGTGATCCGCCTGGTGGCTGGTGAGATGGGCCAGAATGAA
CCAGACCAGGGAGGCCAACGTGGGGTCATCATCAACACTGCCAGTGTGGCTGCCTTCGAG
GGTCAGGTTGGACAAGCTGCATACTCTGCTTCCAAGGGGGGAATAGTGGGCATGACACTG
CCCATTGCTCGGGATCTGGCTCCCATAGGTATCCGGGTGATGACCATTGCCCCAGGTCTG
TTTGGCACCCCACTGCTGACCAGCCTCCCAGAGAAAGTGTGCAACTTCTTGGCCAGCCAA
GTGCCCTTCCCTAGCCGACTGGGTGACCCTGCTGAGTATGCTCACCTCGTACAGGCCATC
ATCGAGAACCCATTCCTCAATGGAGAGGTCATCCGGCTGGATGGGGCCATTCGTATGCAG
CCTTGA
Enzyme 4 GenBank Gene ID U96132 Link Image
Enzyme 4 GeneCard ID HSD17B10 Link Image
Enzyme 4 GenAtlas ID HSD17B10 Link Image
Enzyme 4 HGNC ID HGNC:4800 Link Image
Enzyme 4 Chromosome Location X
Enzyme 4 Locus Xp11.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Yan SD, Fu J, Soto C, Chen X, Zhu H, Al-Mohanna F, Collison K, Zhu A, Stern E, Saido T, Tohyama M, Ogawa S, Roher A, Stern D: An intracellular protein that binds amyloid-beta peptide and mediates neurotoxicity in Alzheimer's disease. Nature. 1997 Oct 16;389(6652):689-95. [PubMed Link Image]
  2. Miller AP, Willard HF: Chromosomal basis of X chromosome inactivation: identification of a multigene domain in Xp11.21-p11.22 that escapes X inactivation. Proc Natl Acad Sci U S A. 1998 Jul 21;95(15):8709-14. [PubMed Link Image]
  3. He XY, Schulz H, Yang SY: A human brain L-3-hydroxyacyl-coenzyme A dehydrogenase is identical to an amyloid beta-peptide-binding protein involved in Alzheimer's disease. J Biol Chem. 1998 Apr 24;273(17):10741-6. [PubMed Link Image]
  4. Ofman R, Ruiter JP, Feenstra M, Duran M, Poll-The BT, Zschocke J, Ensenauer R, Lehnert W, Sass JO, Sperl W, Wanders RJ: 2-Methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency is caused by mutations in the HADH2 gene. Am J Hum Genet. 2003 May;72(5):1300-7. Epub 2003 Apr 14. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5617
Enzyme 5 Name Peroxisomal bifunctional enzyme
Enzyme 5 Synonyms
  1. PBE
  2. PBFE[Includes: Enoyl-CoA hydratase
Enzyme 5 Gene Name EHHADH
Enzyme 5 Protein Sequence >Peroxisomal bifunctional enzyme 
MAEYTRLHNALALIRLRNPPVNAISTTLLRDIKEGLQKAGRDHTIKAIVICGAEGKFSAG
ADIRGFSAPRTFGLILGHVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHADAQV
GLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDPVEE
AIRFAQRVSDQPLESRRLCNKPIQSLPNMDSIFSEALLKMRRQHPGCLAQEACVRAVQAA
VQYPYEVGIKKEEELFLYLLQSGQARALQYAFFAERKANKWSTPSGASWKTASARPVSSV
GVVGLGTMGRGIVISFARARIPVIGVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSG
PKPRLTSSVKELGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIAS
STDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTTIATVMNLSKKIKKIGVVVGNCFGFV
GNRMLNPYYNQAYFLLEEGSKPEEVDQVLEEFGFKMGPFRVSDLAGLDVGWKSRKGQGLT
GPTLLPGTPARKRGNRRYCPIPDVLCELGRFGQKTGKGWYQYDKPLGRIHKPDPWLSTFL
SRYRKPHHIEPRTISQDEILERCLYSLINEAFRILGEGIAASPEHIDVVYLHGYGCARHK
GGPMFYASTVGLPTVLEKLQKYYRQNPDIPQLEPSDYLKKLASQGNPPLKEWQSLAGSPS
SKL
Enzyme 5 Number of Residues 723
Enzyme 5 Molecular Weight 79341
Enzyme 5 Theoretical pI 9.49
Enzyme 5 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
—
Enzyme 5 General Function Lipid transport and metabolism
Enzyme 5 Specific Function (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl- CoA + H(2)O
Enzyme 5 Pathways
Enzyme 5 Reactions
  • (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-23
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 452045 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q08426 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name ECHP_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2172 bp 
ATGGCCGAGTATACGCGGCTGCACAACGCCTTGGCGCTAATCCGCCTCCGAAACCCGCCG
GTCAACGCGATCAGTACGACTTTACTCCGTGATATAAAAGAAGGACTACAGAAAGCTGGA
AGAGACCATACAATAAAAGCCATTGTGATTTGTGGAGCAGAGGGCAAATTTTCTGCAGGT
GCTGATATTCGTGGCTTCAGTGCTCCTAGGACATTTGGCCTTATACTGGGACATGTAGTA
GATGAAATACAGAGAAATGAGAAGCCCGTGGTGGCAGCAATCCAAGGCATGGCTTTCGGA
GGGGGACTAGAGCTGGCCCTGGGCTGTCACTATAGGATTGCCCACGCAGACGCTCAAGTT
GGCTTACCAGAAGTTACACTTGGACTTCTCCCTGGTGCAAGAGGAACCCAGCTTCTCCCC
AGACTCACTGGAGTTCCTGCTGCACTTGACTTAATTACCTCAGGAAGACGTATTTTAGCA
GATGAAGCACTCAAGCTGGGCATTCTAGATAAAGTTGTAAACTCAGACCCGGTTGAAGAA
GCAATCAGATTTGCTCAGAGAGTTTCAGATCAACCTCTAGAATCCCGTAGACTCTGCAAC
AAGCCAATTCAGAGCTTGCCCAACATGGACAGCATTTTTAGTGAGGCCCTCTTGAAGATG
CGGAGGCAGCACCCTGGGTGTCTTGCACAGGAGGCTTGTGTCCGTGCAGTCCAGGCTGCT
GTGCAGTATCCCTATGAAGTGGGCATCAAGAAGGAGGAGGAGCTGTTTCTATATCTTTTG
CAATCAGGGCAGGCTAGAGCCCTGCAATATGCTTTCTTCGCTGAAAGGAAAGCAAATAAG
TGGTCAACTCCCTCCGGAGCATCGTGGAAAACAGCATCAGCGCGGCCTGTCTCCTCAGTT
GGTGTTGTTGGCTTGGGAACAATGGGCCGAGGCATTGTCATTTCTTTTGCAAGGGCCAGG
ATTCCTGTGATTGGTGTAGACTCGGACAAAAACCAGCTAGCAACTGCAAACAAGATGATA
ACCTCTGTCTTGGAAAAAGAAGCCTCCAAAATGCAACAGAGCGGCCACCCTTGGTCAGGA
CCAAAACCCAGGTTAACTTCATCTGTGAAGGAGCTTGGTGGTGTAGATTTAGTCATTGAA
GCAGTATTTGAGGAAATGAGCCTGAAGAAGCAGGTCTTTGCTGAACTCTCAGCTGTGTGC
AAACCAGAAGCATTTTTGTGCACTAATACTTCAGCCCTGGATGTTGATGAGATTGCTTCT
TCCACTGATCGTCCTCACTTGGTCATTGGCACCCACTTCTTTTCGCCAGCTCATGTCATG
AAGTTGTTAGAGGTTATTCCCAGCCAATACTCTTCCCCCACTACCATTGCCACTGTTATG
AACTTATCAAAAAAGATTAAAAAGATTGGAGTCGTTGTAGGCAACTGTTTTGGATTTGTG
GGGAATCGAATGTTGAATCCTTACTACAATCAGGCATATTTCTTGTTAGAAGAAGGCAGC
AAACCAGAGGAGGTAGATCAGGTGCTGGAAGAGTTTGGTTTTAAAATGGGACCTTTTAGA
GTGTCTGATCTTGCTGGGTTGGATGTGGGCTGGAAATCTAGAAAGGGGCAAGGTCTTACT
GGACCTACATTGCTTCCAGGAACTCCTGCCCGAAAAAGGGGTAATAGGAGGTACTGCCCA
ATTCCTGATGTGCTCTGTGAATTAGGACGATTTGGCCAGAAGACAGGTAAGGGTTGGTAT
CAATATGACAAGCCATTGGGTAGGATTCACAAACCTGATCCCTGGCTTTCCACATTCCTA
TCACGGTATAGAAAACCCCATCACATTGAACCACGTACCATTAGCCAGGATGAGATCCTT
GAACGCTGCTTATATTCACTTATCAATGAAGCATTCCGTATCTTGGGAGAAGGGATAGCT
GCTAGCCCAGAGCACATTGATGTTGTCTATTTACATGGATATGGATGCGCAAGGCACAAG
GGCGGGCCCATGTTCTATGCTTCCACAGTTGGGTTGCCCACAGTTCTAGAGAAATTGCAG
AAATATTACAGGCAGAACCCTGATATTCCCCAACTGGAGCCAAGTGACTATCTAAAAAAA
CTGGCTTCTCAGGGAAACCCTCCCCTGAAAGAATGGCAAAGCTTGGCAGGCTCCCCTAGC
AGTAAATTGTGA
Enzyme 5 GenBank Gene ID L07077 Link Image
Enzyme 5 GeneCard ID EHHADH Link Image
Enzyme 5 GenAtlas ID EHHADH Link Image
Enzyme 5 HGNC ID HGNC:3247 Link Image
Enzyme 5 Chromosome Location 3
Enzyme 5 Locus 3q26.3-q28
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Hoefler G, Forstner M, McGuinness MC, Hulla W, Hiden M, Krisper P, Kenner L, Ried T, Lengauer C, Zechner R, et al.: cDNA cloning of the human peroxisomal enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme and localization to chromosome 3q26.3-3q28: a free left Alu Arm is inserted in the 3' noncoding region. Genomics. 1994 Jan 1;19(1):60-7. [PubMed Link Image]
  2. Chen GL, Balfe A, Erwa W, Hoefler G, Gaertner J, Aikawa J, Chen WW: Import of human bifunctional enzyme into peroxisomes of human hepatoma cells in vitro. Biochem Biophys Res Commun. 1991 Aug 15;178(3):1084-91. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5618
Enzyme 6 Name Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial precursor
Enzyme 6 Synonyms
  1. Short chain 3-hydroxyacyl-CoA dehydrogenase
  2. HCDH
  3. Medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase
Enzyme 6 Gene Name HADH
Enzyme 6 Protein Sequence >Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial precursor 
MAFVTRQFMRSVSSSSTASASAKKIIVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTE
DILAKSKKGIEESLRKVAKKKFAENPKAGDEFVEKTLSTIATSTDAASVVHSTDLVVEAI
VENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKL
VEVIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDAS
KEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAEN
KFGKKTGEGFYKYK
Enzyme 6 Number of Residues 314
Enzyme 6 Molecular Weight 34278
Enzyme 6 Theoretical pI 9.41
Enzyme 6 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
—
Enzyme 6 General Function Lipid transport and metabolism
Enzyme 6 Specific Function Plays an essential role in the mitochondrial beta- oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA
Enzyme 6 Pathways
Enzyme 6 Reactions
  • (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + 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 1483511 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q16836 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name HCDH_HUMAN Link Image
Enzyme 6 PDB ID 1F0Y Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >945 bp 
ATGGCCTTCGTCACCAGGCAGTTCATGCGTTCCGTGTCCTCCTCGTCCACCGCCTCGGCC
TCGGCCAAGAAGATAATCGTCAAGCACGTGACGGTCATCGGCGGCGGGCTGATGGGCGCC
GGCATTGCCCAGGTTGCTGCAGCAACTGGTCACACAGTAGTGTTGGTAGACCAGACAGAG
GACATCCTGGCAAAATCCAAAAAGGGAATTGAGGAAAGCCTTAGGAAAGTGGCAAAGAAG
AAGTTTGCAGAAAACCCTAAGGCCGGCGATGAATTTGTGGAGAAGACCCTGAGCACCATA
GCGACCAGCACGGATGCAGCCTCCGTTGTCCACAGCACAGACTTGGTGGTGGAAGCCATC
GTGGAGAATCTGAAGGTGAAAAACGAGCTCTTCAAAAGGCTGGACAAGTTTGCTGCTGAA
CATACAATCTTTGCCAGCAACACTTCCTCCTTGCATATTACAAGCATAGCTAATGCCACC
ACCAGACAAGACCGATTCGCTGGCCTCCATTTCTTCAACCCAGTGCCTGTCATGAAACTT
GTGGAGGTCATTAAAACACCAATGACCAGCCAGAAGACATTTGAATCTTTGGTAGACTTT
AGCAAAGCCCTAGGAAAGCATCCTGTTTCTTGCAAGGACACTCCTGGGTTTATTGTGAAC
CGCCTCCTGGTTCCATACCTCATGGAAGCAATCAGGCTGTATGAACGAGGTGACGCATCC
AAAGAAGACATTGACACTGCTATGAAATTAGGAGCCGGTTACCCCATGGGCCCATTTGAG
CTTCTAGATTATGTCGGACTGGATACTACGAAGTTCATCGTGGATGGGTGGCATGAAATG
GATGCAGAGAACCCATTACATCAGCCCAGCCCATCCTTAAATAAGCTGGTAGCAGAGAAC
AAGTTCGGCAAGAAGACTGGAGAAGGATTTTACAAATACAAGTGA
Enzyme 6 GenBank Gene ID X96752 Link Image
Enzyme 6 GeneCard ID HADH Link Image
Enzyme 6 GenAtlas ID HADH Link Image
Enzyme 6 HGNC ID HGNC:4799 Link Image
Enzyme 6 Chromosome Location 4
Enzyme 6 Locus 4q22-q26
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Vredendaal PJ, van den Berg IE, Malingre HE, Stroobants AK, Olde Weghuis DE, Berger R: Human short-chain L-3-hydroxyacyl-CoA dehydrogenase: cloning and characterization of the coding sequence. Biochem Biophys Res Commun. 1996 Jun 25;223(3):718-23. [PubMed Link Image]
  2. Barycki JJ, O'Brien LK, Bratt JM, Zhang R, Sanishvili R, Strauss AW, Banaszak LJ: Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism. Biochemistry. 1999 May 4;38(18):5786-98. [PubMed Link Image]
  3. Barycki JJ, O'Brien LK, Strauss AW, Banaszak LJ: Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase. J Biol Chem. 2000 Sep 1;275(35):27186-96. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5626
Enzyme 7 Name Trifunctional enzyme subunit alpha, mitochondrial precursor
Enzyme 7 Synonyms
  1. TP-alpha
  2. 78 kDa gastrin-binding protein[Includes: Long-chain enoyl-CoA hydratase
Enzyme 7 Gene Name HADHA
Enzyme 7 Protein Sequence >Trifunctional enzyme subunit alpha, mitochondrial precursor 
MVACRAIGILSRFSAFRILRSRGYICRNFTGSSALLTRTHINYGVKGDVAVVRINSPNSK
VNTLSKELHSEFSEVMNEIWASDQIRSAVLISSKPGCFIAGADINMLAACKTLQEVTQLS
QEAQRIVEKLEKSTKPIVAAINGSCLGGGLEVAISCQYRIATKDRKTVLGTPEVLLGALP
GAGGTQRLPKMVGVPAALDMMLTGRSIRADRAKKMGLVDQLVEPLGPGLKPPEERTIEYL
EEVAITFAKGLADKKISPKRDKGLVEKLTAYAMTIPFVRQQVYKKVEEKVRKQTKGLYPA
PLKIIDVVKTGIEQGSDAGYLCESQKFGELVMTKESKALMGLYHGQVLCKKNKFGAPQKD
VKHLAILGAGLMGAGIAQVSVDKGLKTILKDATLTALDRGQQQVFKGLNDKVKKKALTSF
ERDSIFSNLTGQLDYQGFEKADMVIEAVFEDLSLKHRVLKEVEAVIPDHCIFASNTSALP
ISEIAAVSKRPEKVIGMHYFSPVDKMQLLEIITTEKTSKDTSASAVAVGLKQGKVIIVVK
DGPGFYTTRCLAPMMSEVIRILQEGVDPKKLDSLTTSFGFPVGAATLVDEVGVDVAKHVA
EDLGKVFGERFGGGNPELLTQMVSKGFLGRKSGKGFYIYQEGVKRKDLNSDMDSILASLK
LPPKSEVSSDEDIQFRLVTRFVNEAVMCLQEGILATPAEGDIGAVFGLGFPPCLGGPFRF
VDLYGAQKIVDRLKKYEAAYGKQFTPCQLLADHANSPNKKFYQ
Enzyme 7 Number of Residues 763
Enzyme 7 Molecular Weight 83001
Enzyme 7 Theoretical pI 9.52
Enzyme 7 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
—
Enzyme 7 General Function Lipid transport and metabolism
Enzyme 7 Specific Function Bifunctional subunit
Enzyme 7 Pathways
Enzyme 7 Reactions
  • (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-23
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 862457 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P40939 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name ECHA_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2292 bp 
ATGGTGGCCTGCCGGGCGATTGGCATCCTCAGCCGCTTTTCTGCCTTCAGGATCCTCCGC
TCCCGAGGTTATATATGCCGCAATTTTACAGGGTCTTCTGCTTTGCTGACCAGAACCCAT
ATTAACTATGGAGTCAAAGGGGATGTGGCAGTTGTTCGAATTAACTCTCCCAATTCAAAG
GTAAATACACTGAGTAAAGAGCTACATTCAGAGTTCTCAGAAGTTATGAATGAAATCTGG
GCTAGTGATCAAATCAGAAGTGCCGTCCTTATCTCATCAAAGCCAGGCTGCTTTATTGCA
GGTGCTGATATCAACATGTTAGCCGCTTGCAAGACCCTTCAAGAAGTAACACAGCTATCA
CAAGAAGCACAGAGAATAGTTGAGAAACTTGAAAAGTCCACAAAGCCTATTGTGGCTGCC
ATCAATGGATCCTGCGTGGGAGGAGGACTTGAGGTTGCCATTTCATGCCAATACAGAATA
GCAACAAAAGACAGAAAAACAGTATTAGGTACCCCTGAAGTTTTGCTGGGGGCCTTACCA
GGAGCAGGAGGCACACAAAGGCTGCCCAAAATGGTGGGTGTGCCTGCTGCTTTGGACATG
ATGCTGACTGGTAGAAGCATTCGTGCAGACAGGGCAAAGAAAATGGGACTGGTTGACCAA
CTGGTGGAACCCCTGGGACCAGGACTAAAACCTCCAGAGGAACGGACAATAGAATACCTA
GAAGAAGTTGCAATTACTTTTGCCAAAGGACTAGCTGATAAGAAGATCTCTCCAAAGAGA
GACAAGGGATTGGTGGAAAAATTGACAGCGTATGCCATGACTATTCCATTTGTCAGGCAA
CAGGTTTACAAAAAAGTGGAAGAAAAAGTGCGAAAGCAGACTAAAGGCCTTTATCCTGCA
CCTCTGAAAATAATTGATGTGGTAAAGACTGGAATTGAGCAAGGGAGTGATGCCGGTTAT
CTCTGTGAATCTCAGAAATTTGGAGAGCTTGTAATGACCAAAGAATCAAAGGCCTTGATG
GGACTCTACCATGGTCAGGTCCTGTGCAAGAAGAATAAATTTGGAGCTCCACAGAAGGAT
GTTAAGCATCTGGCTATTCTTGGTGCAGGGCTGATGGGAGCAGGCATCGCCCAAGTCTCC
GTGGATAAGGGGCTAAAGACTATACTTAAAGATGCCACCCTCACTGCGCTAGACCGAGGA
CAGCAACAAGTGTTCAAAGGATTGAATGACAAAGTGAAGAAGAAAGCTCTAACATCATTT
GAAAGGGATTCCATCTTCAGCAACTTGACTGGGCAGCTTGATTACCAAGGTTTTGAAAAG
GCCGACATGGTGATTGAAGCTGTGTTTGAGGACCTTAGTCTTAAGCACAGAGTGCTAAAG
GAAGTAGAAGCGGTGATTCCAGATCACTGTATCTTTGCCAGTAACACATCTGCTCTCCCA
ATCAGTGAAATCGCTGCTGTCAGCAAAAGACCTGAGAAGGTGATTGGCATGCACTACTTC
TCTCCCGTGGACAAGATGCAGCTGCTGGAGATTATCACGACCGAGAAAACTTCCAAAGAC
ACCAGTGCTTCAGCTGTAGCAGTTGGTCTCAAGCAGGGGAAGGTCATCATTGTGGTTAAG
GATGGACCTGGCTTCTATACTACCAGGTGTCTTGCGCCCATGATGTCTGAAGTCATCCGA
ATCCTCCAGGAAGGAGTTGACCCGAAGAAGCTGGATTCCCTGACCACAAGCTTTGGCTTT
CCTGTGGGTGCCGCCACACTGGTGGATGAAGTTGGTGTGGATGTAGCGAAACATGTGGCG
GAAGATCTGGGCAAAGTCTTTGGGGAGCGGTTTGGAGGTGGAAACCCAGAACTGCTGACA
CAGATGGTGTCCAAGGGCTTCCTAGGTCGTAAATCTGGGAAGGGCTTTTACATCTATCAG
GAGGGTGTGAAGAGGAAGGATTTGAATTCTGACATGGATAGTATTTTAGCGAGTCTGAAG
CTGCCTCCTAAGTCTGAAGTCTCATCAGACGAAGACATCCAGTTCCGCCTGGTGACAAGA
TTTGTGAATGAGGCAGTCATGTGCCTGCAAGAGGGGATCTCGGCCACACCTGCAGAGGGA
GACATCGGAGCCGTCTTTGGGCTTGGCTTCCCGCCTTGTCTGGGAGGGCCTTTCCGCTTT
GTGGATCTGTATGGCGCCCAGAAGATAGTGGACCGGCTCAAGAAATATGAAGCTGCCTAT
GGAAAACAGTTCACCCCATGCCAGCTGCTAGCTGACCATGCTAACAGCCCTAACAAGAAG
TTCTACCAGTGA
Enzyme 7 GenBank Gene ID D16480 Link Image
Enzyme 7 GeneCard ID HADHA Link Image
Enzyme 7 GenAtlas ID HADHA Link Image
Enzyme 7 HGNC ID HGNC:4801 Link Image
Enzyme 7 Chromosome Location 2
Enzyme 7 Locus 2p23
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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. Zhang QX, Baldwin GS: Structures of the human cDNA and gene encoding the 78 kDa gastrin-binding protein and of a related pseudogene. Biochim Biophys Acta. 1994 Oct 18;1219(2):567-75. [PubMed Link Image]
  3. Sims HF, Brackett JC, Powell CK, Treem WR, Hale DE, Bennett MJ, Gibson B, Shapiro S, Strauss AW: The molecular basis of pediatric long chain 3-hydroxyacyl-CoA dehydrogenase deficiency associated with maternal acute fatty liver of pregnancy. Proc Natl Acad Sci U S A. 1995 Jan 31;92(3):841-5. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5716
Enzyme 8 Name Peroxisomal multifunctional enzyme type 2
Enzyme 8 Synonyms
  1. MFE-2
  2. D-bifunctional protein
  3. DBP
  4. 17-beta-hydroxysteroid dehydrogenase 4
  5. 17-beta-HSD 4
  6. D-3-hydroxyacyl-CoA dehydratase
  7. 3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase
  8. 3- hydroxyacyl-CoA dehydrogenase
Enzyme 8 Gene Name HSD17B4
Enzyme 8 Protein Sequence >Peroxisomal multifunctional enzyme type 2 
MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVE
EIRRRGGKAVANYDSVEEGEKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIH
RVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAKLGLLGLANSLAI
EGRKSNIHCNTIAPNAGSRMTQTVMPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVG
AGWIGKLRWERTLGAIVRQKNHPMTPEAVKANWKKICDFENASKPQSIQESTGSIIEVLS
KIDSEGGVSANHTSRATSTATSGFAGAIGQKLPPFSYAYTELEAIMYALGVGASIKDPKD
LKFIYEGSSDFSCLPTFGVIIGQKSMMGGGLAEIPGLSINFAKVLHGEQYLELYKPLPRA
GKLKCEAVVADVLDKGSGVVIIMDVYSYSEKELICHNQFSLFLVGSGGFGGKRTSDKVKV
AVAIPNRPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFS
ARRVLQQFADNDVSRFKAIKARFAKPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISN
AYVDLAPTSGTSAKTPSEGGKLQSTFVFEEIGRRLKDIGPEVVKKVNAVFEWHITKGGNI
GAKWTIDLKSGSGKVYQGPAKGAADTTIILSDEDFMEVVLGKLDPQKAFFSGRLKARGNI
MLSQKLQMILKDYAKL
Enzyme 8 Number of Residues 736
Enzyme 8 Molecular Weight 79687
Enzyme 8 Theoretical pI 9.21
Enzyme 8 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
  • steroid binding
  • sterol carrier activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 8 General Function Lipid transport and metabolism
Enzyme 8 Specific Function Bifunctional enzyme acting on the peroxisomal beta- oxidation pathway for fatty acids. Catalyzes the formation of 3- ketoacyl-CoA intermediates from both straight-chain and 2-methyl- branched-chain fatty acids
Enzyme 8 Pathways
Enzyme 8 Reactions
  • (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 1050517 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P51659 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name DHB4_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >2211 bp 
ATGGGCTCACCGCTGAGGTTCGACGGGCGGGTGGTACTGGTCACCGGCGCGGGGGCAGGA
TTGGGCCGAGCCTATGCCCTGGCTTTTGCAGAAAGAGGAGCGTTAGTTGTTGTGAATGAT
TTGGGAGGGGACTTCAAAGGAGTTGGTAAAGGCTCCTTAGCTGCTGATAAGGTTGTTGAA
GAAATAAGAAGGAGAGGTGGAAAAGCAGTGGCCAACTATGATTCAGTGGAAGAAGGAGAG
AAGGTTGTGAAGACAGCCCTGGATGCTTTTGGAAGAATAGATGTTGTGGTCAACAATGCT
GGAATTCTGAGGGATCGTTCCTTTGCTAGGATAAGTGATGAAGACTGGGATATAATCCAC
AGAGTTCATTTGCGGGGTTCATTCCAAGTGACACGGGCAGCATGGGAACACATGAAGAAA
CAGAAGTATGGAAGGATTATTATGACTTCATCAGCTTCAGGAATATATGGCAACTTTGGC
CAGGCCAATTATAGTGCTGCAAAGTTGGGTCTTCTGGGCCTTGCAAATTCTCTTGCAATT
GAAGGCAGGAAAAGCAACATTCATTGTAACACCATTGCTCCTAATGCGGGATCACGGATG
ACTCAGACAGTTATGCCTGAAGATCTTGTGGAAGCCCTGAAGCCAGAGTATGTGGCACCT
CTTGTCCTTTGGCTTTGTCACGAGAGTTGTGAGGAGAATGGTGGCTTGTTTGAGGTTGGA
GCAGGATGGATTGGAAAATTACGCTGGGAGCGGACTCTTGGAGCTATTGTAAGACAAAAG
AATCACCCAATGACTCCTGAGGCAGTCAAGGCTAACTGGAAGAAGATCTGTGACTTTGAG
AATGCCAGCAAGCCTCAGAGTATCCAAGAATCAACTGGCAGTATAATTGAAGTTCTGAGT
AAAATAGATTCAGAAGGAGGAGTTTCAGCAAATCATACTAGTCGTGCAACGTCTACAGCA
ACATCAGGATTTGCTGGAGCTATTGGCCAGAAACTCCCTCCATTTTCTTATGCTTATACG
GAACTGGAAGCTATTATGTATGCCCTTGGAGTGGGAGCGTCAATCAAGGATCCAAAAGAT
TTGAAATTTATTTATGAAGGAAGTTCTGATTTCTCCTGTTTGCCCACCTTCGGAGTTATC
ATAGGTCAGAAATCTATGATGGGTGGAGGATTAGCAGAAATTCCTGGACTTTCAATCAAC
TTTGCAAAGGTTCTTCATGGAGAGCAGTACTTAGAGTTATATAAACCACTTCCCAGAGCA
GGAAAATTAAAATGTGAAGCAGTTGTTGCTGATGTCCTAGATAAAGGATCCGGTGTAGTG
ATTATTATGGATGTCTATTCTTATTCTGAGAAGGAACTTATATGCCACAATCAGTTCTCT
CTCTTTCTTGTTGGCTCTGGAGGCTTTGGTGGAAAACGGACATCAGACAAAGTCAAGGTA
GCTGTAGCCATACCTAATAGACCTCCTGATGCTGTACTTACAGATACCACCTCTCTTAAT
CAGGCTGCTTTGTACCGCCTCAGTGGAGACTGGAATCCCTTACACATTGATCCTAACTTT
GCTAGTCTAGCAGGTTTTGACAAGCCCATATTACATGGATTATGTACATTTGGATTTTCT
GCCAGGCGTGTGTTACAGCAGTTTGCAGATAATGATGTGTCAAGATTCAAGGCAATTAAG
GCTCGTTTTGCAAAACCAGTATATCCAGGACAAACTCTACAAACTGAGATGTGGAAGGAA
GGAAACAGAATTCATTTTCAAACCAAGGTCCAAGAAACTGGAGACATTGTCATTTCAAAT
GCATATGTGGATCTTGCACCAACATCTGGTACTTCAGCTAAGACACCCTCTGAGGGCGGG
AAGCTTCAGAGTACCTTTGTATTTGAGGAAATAGGACGCCGCCTAAAGGATATTGGGCCT
GAGGTGGTGAAGAAAGTAAATGCTGTATTTGAGTGGCATATAACCAAAGGCGGAAATATT
GGGGCTAAGTGGACTATTGACCTGAAAAGTGGTTCTGGAAAAGTGTACCAAGGCCCTGCA
AAAGGTGCTGCTGATACAACAATCATACTTTCAGATGAAGATTTCATGGAGGTGGTCCTG
GGCAAGCTTGACCCTCAGAAGGCATTCTTTAGTGGCAGGCTGAAGGCCAGAGGGAACATC
ATGCTGAGCCAGAAACTTCAGATGATTCTTAAAGACTACGCCAAGCTCTGA
Enzyme 8 GenBank Gene ID X87176 Link Image
Enzyme 8 GeneCard ID HSD17B4 Link Image
Enzyme 8 GenAtlas ID HSD17B4 Link Image
Enzyme 8 HGNC ID HGNC:5213 Link Image
Enzyme 8 Chromosome Location 5
Enzyme 8 Locus 5q21
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Adamski J, Normand T, Leenders F, Monte D, Begue A, Stehelin D, Jungblut PW, de Launoit Y: Molecular cloning of a novel widely expressed human 80 kDa 17 beta-hydroxysteroid dehydrogenase IV. Biochem J. 1995 Oct 15;311 ( Pt 2):437-43. [PubMed Link Image]
  2. Jiang LL, Miyazawa S, Souri M, Hashimoto T: Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein. J Biochem (Tokyo). 1997 Feb;121(2):364-9. [PubMed Link Image]
  3. Leenders F, Dolez V, Begue A, Moller G, Gloeckner JC, de Launoit Y, Adamski J: Structure of the gene for the human 17beta-hydroxysteroid dehydrogenase type IV. Mamm Genome. 1998 Dec;9(12):1036-41. [PubMed Link Image]
  4. Jiang LL, Kobayashi A, Matsuura H, Fukushima H, Hashimoto T: Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase. J Biochem (Tokyo). 1996 Sep;120(3):624-32. [PubMed Link Image]
  5. Haapalainen AM, van Aalten DM, Merilainen G, Jalonen JE, Pirila P, Wierenga RK, Hiltunen JK, Glumoff T: Crystal structure of the liganded SCP-2-like domain of human peroxisomal multifunctional enzyme type 2 at 1.75 A resolution. J Mol Biol. 2001 Nov 9;313(5):1127-38. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 8815
Enzyme 9 Name Hydroxyacyl-Coenzyme A dehydrogenase, type II
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name HADH2
Enzyme 9 Protein Sequence >Hydroxyacyl-Coenzyme A dehydrogenase, type II 
MAAACRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVF
APADVTSEKDVQTALALAKGKFGRVDVAVNCAGIAVASKTYNLKKGQTHTLEDFQRVLDV
NLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTL
PIARDLAPIGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNGE
VIRLDGAIRMQP
Enzyme 9 Number of Residues 252
Enzyme 9 Molecular Weight 25984
Enzyme 9 Theoretical pI 7.29
Enzyme 9 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • 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
  • 1-27
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 57210025 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q5H927 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name Q5H927_HUMAN Link Image
Enzyme 9 PDB ID 1SO8 Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >759 bp 
ATGGCAGCAGCGTGTCGGAGCGTGAAGGGCCTGGTGGCGGTAATAACCGGAGGAGCCTCG
GGCCTGGGCCTGGCCACGGCGGAGCGACTTGTGGGGCAGGGAGCCTCTGCTGTGCTTCTG
GACCTGCCCAACTCGGGTGGGGAGGCCCAAGCCAAGAAGTTAGGAAACAACTGCGTTTTC
GCCCCAGCCGACGTGACCTCTGAGAAGGATGTGCAAACAGCTCTGGCTCTAGCAAAAGGA
AAGTTTGGCCGTGTGGATGTAGCTGTCAACTGTGCAGGCATCGCGGTGGCTAGCAAGACG
TACAACTTAAAGAAGGGCCAGACCCATACCTTGGAAGACTTCCAGCGAGTTCTTGATGTG
AATCTCATGGGCACCTTCAATGTGATCCGCCTGGTGGCTGGTGAGATGGGCCAGAATGAA
CCAGACCAGGGAGGCCAACGTGGGGTCATCATCAACACTGCCAGTGTGGCTGCCTTCGAG
GGTCAGGTTGGACAAGCTGCATACTCTGCTTCCAAGGGGGGAATAGTGGGCATGACACTG
CCCATTGCTCGGGATCTGGCTCCCATAGGTCTGTTTGGCACCCCACTGCTGACCAGCCTC
CCAGAGAAAGTGTGCAACTTCTTGGCCAGCCAAGTGCCCTTCCCTAGCCGACTGGGTGAC
CCTGCTGAGTATGCTCACCTCGTACAGGCCATCATCGAGAACCCATTCCTCAATGGAGAG
GTCATCCGGCTGGATGGGGCCATTCGTATGCAGCCTTGA
Enzyme 9 GenBank Gene ID Z97054 Link Image
Enzyme 9 GeneCard ID HADH2 Link Image
Enzyme 9 GenAtlas ID HADH2 Link Image
Enzyme 9 HGNC ID HGNC:4800 Link Image
Enzyme 9 Chromosome Location X
Enzyme 9 Locus Xp11.2
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 13010
Enzyme 10 Name Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase
Enzyme 10 Synonyms
  1. Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase, isoform CRA_b
  2. Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase variant
Enzyme 10 Gene Name EHHADH
Enzyme 10 Protein Sequence >Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase 
MAEYTRLHNALALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAG
ADIRGFSAPRTFGLTLGHVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQV
GLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDPVEE
AIRFAQRVSDQPLESRRLCNKPIQSLPNMDSIFSEALLKMRRQHPGCLAQEACVRAVQAA
VQYPYEVGIKKEEELFLYLLQSGQARALQYAFFAERKANKWSTPSGASWKTASARPVSSV
GVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSG
PKPRLTSSVKELGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIAS
STDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTTIATVMNLSKKIKKIGVVVGNCFGFV
GNRMLNPYYNQAYFLLEEGSKPEEVDQVLEEFGFKMGPFRVSDLAGLDVGWKSRKGQGLT
GPTLLPGTPARKRGNRRYCPIPDVLCELGRFGQKTGKGWYQYDKPLGRIHKPDPWLSKFL
SRYRKTHHIEPRTISQDEILERCLYSLINEAFRILGEGIAASPEHIDVVYLHGYGWPRHK
GGPMFYASTVGLPTVLEKLQKYYRQNPDIPQLEPSDYLKKLASQGNPPLKEWQSLAGSPS
SKL
Enzyme 10 Number of Residues 723
Enzyme 10 Molecular Weight 79496
Enzyme 10 Theoretical pI 9.54
Enzyme 10 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
—
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 62021246 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q58EZ5 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name Q58EZ5_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 BC038948 Link Image
Enzyme 10 GeneCard ID Q58EZ5 Link Image
Enzyme 10 GenAtlas ID EHHADH Link Image
Enzyme 10 HGNC ID HGNC:3247 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
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]
  2. Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed Link Image]
  3. Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 13022
Enzyme 11 Name Putative uncharacterized protein
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name HADHA
Enzyme 11 Protein Sequence >Putative uncharacterized protein 
MVACRAIGILSRFSAFRILRSRGYICRNFTGSSALLTRTHINYGVKGDVAVVRINSPNSK
VNTLSKELHSEFSEVMNEIWASDQIRSAVLISSKPGCFIAGADINMLAACKTLQEVTQLS
QEAQRIVEKLEKSTKPIVAAINGSCLGGGLEVAISCQYRIATKDRKTVLGTPEVLLGALP
GAGGTQRLPKMVGVPAALDMMLTGRSIRADRAKKMGLVDQLVEPLGPGLKPPEERTIEYL
EEVAITFAKGLADKKISPKRDKGLVEKLTAYAMTIPFVRQQVYKKVEEKVRKQTKGLYPA
PLKIIDVVKTGIEQGSDAGYLCESQKFGELVMTKESKALMGLYHGQVLCKKNKFGAPQKD
VKHLAILGAGLMGAGIAQVSVDKGLKTILKDATLTALDRGQQQVFKGLNDKVKKKALTSF
ERDSIFSNLTGQLDYQGFEKADMVIEAVFEDLSLKHRVLKEVEAVIPDHCIFASNTSALP
ISEIAAVSKRPEKVIGMHYFSPVDKMQLLEIITTEKTSKDTSASAVAVGLKQGKVIIVVK
DGPGFYTTRCLAPMMSEVIRILQEGVDPKKLDSLTTSFGFPVGAATLVDEVGVDVAKHVA
EDLGKVFGERFGGGNPELLTQMVSKGFLGRKSGKGFYIYQEGVKRKDLNSDMDSILASLK
LPPKSEVSSDEDIQFRLVTRFVNEAVMCLQEGILATPAEGDIGAVFGLGFPPCLGGPFRF
VDLYGAQKIVDRLKKYEAAYGKQFTPCQLLADHANSPNKKFYQ
Enzyme 11 Number of Residues 763
Enzyme 11 Molecular Weight 83000
Enzyme 11 Theoretical pI Not Available
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 B2R7L4 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name B2R7L4_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID Not Available
Enzyme 11 GeneCard ID B2R7L4 Link Image
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
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 14588
Enzyme 12 Name Estradiol 17-beta-dehydrogenase 12
Enzyme 12 Synonyms
  1. 17-beta-HSD 12
  2. 17- beta-hydroxysteroid dehydrogenase 12
  3. 3-ketoacyl-CoA reductase
  4. KAR
Enzyme 12 Gene Name HSD17B12
Enzyme 12 Protein Sequence >Estradiol 17-beta-dehydrogenase 12 
MESALPAAGFLYWVGAGTVAYLALRISYSLFTALRVWGVGNEAGVGPGLGEWAVVTGSTD
GIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASEDIYDKIKT
GLAGLEIGILVNNVGMSYEYPEYFLDVPDLDNVIKKMININILSVCKMTQLVLPGMVERS
KGAILNISSGSGMLPVPLLTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLA
KIRKPTLDKPSPETFVKSAIKTVGLQSRTNGYLIHALMGSIISNLPSWIYLKIVMNMNKS
TRAHYLKKTKKN
Enzyme 12 Number of Residues 312
Enzyme 12 Molecular Weight 34325
Enzyme 12 Theoretical pI 9.79
Enzyme 12 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Catalyzes the transformation of estrone (E1) into estradiol (E2), suggesting a central role in estrogen formation. Its strong expression in ovary and mammary gland suggest that it may constitute the major enzyme responsible for the conversion of E1 to E2 in women. Also has 3-ketoacyl-CoA reductase activity, reducing both long chain 3-ketoacyl-CoAs and long chain fatty acyl-CoAs, suggesting a role in long fatty acid elongation
Enzyme 12 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 12 Reactions
  • estradiol-17beta + NAD(P)+ = estrone + NAD(P)H + H+ [RN:R02352 R02353] ALL_REAC R02352 R02353
  • (other) R04681 R04682
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-29
Enzyme 12 Transmembrane Regions
  • 4-24 182-202 271-291
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 5531815 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q53GQ0 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name DHB12_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >939 bp 
ATGGAGAGCGCTCTCCCCGCCGCCGGCTTCCTGTACTGGGTCGGCGCGGGCACCGTGGCC
TACCTAGCCCTGCGTATTTCGTACTCGCTCTTCACGGCCCTCCGGGTCTGGGGAGTGGGG
AATGAGGCGGGGGTCGGCCCGGGGCTCGGAGAGTGGGCAGTTGTCACAGGTAGTACTGAT
GGAATTGGAAAATCATATGCAGAAGAGTTAGCAAAGCATGGAATGAAGGTTGTCCTTATC
AGCAGATCAAAGGATAAACTTGACCAGGTTTCCAGTGAAATAAAAGAAAAATTCAAAGTG
GAGACAAGAACCATTGCTGTTGACTTTGCATCAGAAGATATTTATGATAAAATTAAAACA
GGCTTGGCTGGTCTTGAAATCGGCATCTTAGTGAACAACGTGGGAATGTCGTATGAGTAT
CCTGAATACTTTTTGGATGTTCCTGACTTGGACAATGTGATCAAGAAAATGATAAATATT
AATATTCTTTCTGTTTGTAAGATGACACAATTGGTACTGCCTGGCATGGTGGAAAGATCC
AAAGGGGCTATTCTGAACATTTCATCTGGCAGTGGCATGCTCCCTGTCCCACTCTTGACC
ATCTATTCTGCAACCAAGACTTTTGTAGATTTCTTCTCTCAGTGCCTCCATGAGGAGTAT
AGGAGCAAGGGCGTCTTTGTGCAGAGTGTCCTGCCATACTTCGTAGCTACAAAACTGGCT
AAAATCCGGAAGCCAACTTTGGATAAGCCCTCTCCGGAGACGTTTGTGAAGTCTGCAATT
AAAACAGTCGGCCTGCAATCCCGAACCAATGGATACCTGATCCATGCTCTTATGGGCTCG
ATAATCTCAAACCTGCCTTCTTGGATTTATTTGAAAATAGTCATGAATATGAACAAGTCT
ACACGGGCTCACTATCTGAAGAAAACCAAGAAGAACTAA
Enzyme 12 GenBank Gene ID AF078850 Link Image
Enzyme 12 GeneCard ID Q53GQ0 Link Image
Enzyme 12 GenAtlas ID HSD17B12 Link Image
Enzyme 12 HGNC ID HGNC:18646 Link Image
Enzyme 12 Chromosome Location 11
Enzyme 12 Locus 11p11.2
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 15876
Enzyme 13 Name ACAA1 protein
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name Not Available
Enzyme 13 Protein Sequence >ACAA1 protein 
MQRLQVVLGHLRGPADSGWMPQAAPCLSGAPQASAADVVVVHGRRTAICRAGRGGFKDTT
PDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPETVPLSTVN
RQCSSGLQAVASIAGGIRNGSYDIGMACGITSENVAERFGISREKQDTFALASQQKAARA
QSKGCFQAEIVPVTTTVHDDKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAG
LTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGARQAITLLNE
LKRRGKRAYGVVSMCIGTGMGAAAVFEYPGN
Enzyme 13 Number of Residues 331
Enzyme 13 Molecular Weight 34637
Enzyme 13 Theoretical pI 8.49
Enzyme 13 GO Classification Not Available
Enzyme 13 General Function Lipid transport and metabolism
Enzyme 13 Specific Function Not Available
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 Q96CA6 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name Q96CA6_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 BC014474 Link Image
Enzyme 13 GeneCard ID Q96CA6 Link Image
Enzyme 13 GenAtlas ID ACAA1 Link Image
Enzyme 13 HGNC ID HGNC:82 Link Image
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs Not Available
Enzyme 13 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 16712
Enzyme 14 Name cDNA FLJ30111 fis, clone BNGH42000360, highly similar to 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16)
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name Not Available
Enzyme 14 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 14 Number of Residues 397
Enzyme 14 Molecular Weight 41897
Enzyme 14 Theoretical pI 8.21
Enzyme 14 GO Classification Not Available
Enzyme 14 General Function Lipid transport and metabolism
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways Not Available
Enzyme 14 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 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 B3KNP8 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name B3KNP8_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 AK054673 Link Image
Enzyme 14 GeneCard ID B3KNP8 Link Image
Enzyme 14 GenAtlas ID Not Available
Enzyme 14 HGNC ID Not Available
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
Enzyme 14 SNPs Not Available
Enzyme 14 General References Not Available
Enzyme 14 Metabolite References Not Available