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Human Metabolome Database Version 2.5

 

Showing metabocard for Pantetheine 4'-phosphate (HMDB01416)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-07-13 11:40:53
Accession Number HMDB01416
Secondary Accession Numbers Not Available
Common Name Pantetheine 4'-phosphate
Description 4'-phosphopantetheine is a metabolite in the pantothenate and coenzyme A biosynthesis pathway. It can be generated from Pantatheine (via pantothenate kinase 1) or R-4'-Phospho-pantothenoyl-L-cysteine (via phosphopantothenoylcysteine decarboxylase) or Dephospho-CoA (via 4'-phosphopantetheine adenylyl-transferase and ectonucleotide pyrophosphatase). In most mammals, coenzyme A can be hydrolyzed to pantetheine and pantothenate in the intestinal lumen via the following series of reactions: coenzyme A leads to phosphopantetheine leads to pantetheine leads to pantothenate. The conversion of 4'-phosphopantetheine (4'-PP) to dephospho-CoA, is catalyzed by 4'-phosphopantetheine adenylyl-transferase. In mammalian systems, this step may occur in the mitochondria or in the cytosol. (PMID: 1746161) It has been identified as an essential cofactor in in the biosynthesis of fatty acids, polyketides, depsipeptides, peptides, and compounds derived from both carboxylic and amino acid precursors. In particular it is a key prosthetic group of acyl carrier protein (ACP) and peptidyl carrier proteins (PCP) and aryl carrier proteins (ArCP) derived from Coenzyme A. Phosphopantetheine fulfils two demands. Firstly, the intermediates remain covalently linked to the synthases (or synthetases) in an energy-rich thiol ester linkage. Secondly, the flexibility and length of phosphopantetheine chain (approximately 2 nm) allows the covalently tethered intermediates to have access to spatially distinct enzyme active sites.
Synonyms
  1. 4'-Phosphopantetheine
  2. Pantetheine 4'-phosphate
  3. Pantetheine 4'-phosphic acid
  4. pantotheine-4'-phosphate
  5. phospho-pantotheine
  6. 4'-phosphopantotheine
  7. Phosphopantetheine
  8. D-Pantetheine 4'-phosphate
Chemical IUPAC Name [3-hydroxy-2,2-dimethyl-3-[2-(2-sulfanylethylcarbamoyl)ethylcarbamoyl]propoxy]phosphonic acid
Chemical Formula C11H23N2O7PS
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Amino Ketones
  • Amino Acid Phosphates
  • Sulanyl Compounds
Sub Class
  • Tetrapeptides
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • secondary carboxylic acid amide
  • thiol (sulfanyl compound)
  • alkylthiol
  • phosphoric acid ester
Biofunction
  • Component of Pantothenate and CoA biosynthesis
Application
—
Source
  • Endogenous
Average Molecular Weight 358.348
Monoisotopic Molecular Weight 358.096344
Isomeric SMILES CC(C)(COP(O)(O)=O)C(O)C(=O)NCCC(=O)NCCS
Canonical SMILES CC(C)(COP(O)(O)=O)C(O)C(=O)NCCC(=O)NCCS
KEGG Compound ID C01134 Link Image
BioCyc ID PANTETHEINE-P Link Image
BiGG ID 36886 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01416 Link Image
Metagene Link HMDB01416 Link Image
METLIN ID Not Available
PubChem Compound 987 Link Image
PubChem Substance 8150907 Link Image
ChEBI ID 16858 Link Image
CAS Registry Number 2226-71-3
InChI Identifier InChI=1/C11H23N2O7PS/c1-11(2,7-20-21(17,18)19)9(15)10(16)13-4-3-8(14)12-5-6-22/h9,15,22H,3-7H2,1-2H3,(H,12,14)(H,13,16)(H2,17,18,19)
Synthesis Reference Masuda, Toru; Fujii, Shoichiro; Takanohashi, Kunio. Pantetheine 4'-phosphate. Jpn. Tokkyo Koho (1971), 3 pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.375 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.71 [Predicted by ALOGPS]; -2.1 [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 1H1T 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
  • Cytoplasm (Predicted from LogP)
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
Pantothenate and CoA Biosynthesis SMP00027 Link Image map00770 Link Image
General References Not Available
Metabolic Enzymes
  1. Fatty acid synthase
  2. Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
  3. Acyl carrier protein, mitochondrial precursor
  4. Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
  5. Pantothenate kinase 4
  6. Pantothenate kinase 1
  7. Pantothenate kinase 3
  8. Bifunctional coenzyme A synthase
  9. Phosphopantothenoylcysteine decarboxylase
  10. Probable 10-formyltetrahydrofolate dehydrogenase ALDH1L2
  11. Pantothenate kinase 2 (Hallervorden-Spatz syndrome) (HCG39342, isoform CRA_c)
  12. FASN variant protein
  13. Acyl carrier protein
Enzyme 1 [top]
Enzyme 1 ID 5264
Enzyme 1 Name Fatty acid synthase
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name FASN
Enzyme 1 Protein Sequence >Fatty acid synthase 
MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRF
DASFFGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEAL
SRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQC
PAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLAR
RVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVG
DPQELNGITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFH
SPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATL
PRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGP
EVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLS
TDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAV
LAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFE
FVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEA
QWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCT
IIPLMKKDHRDNLEFFLAGIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSL
AWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVWKTLA
RALGLGVEQLPVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQ
WDDPDPRLFDHPESPTPNPTEPLFLAQAEVYKELRLRGYDYGPHFQGILEASLEGDSGRL
LWKDNWVSFMDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQDKAQVADVVV
SRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQL
CKGLVQALQTTVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQ
VLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLL
SPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVA
ALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESL
FSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRP
VWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGD
LVMNVYRDGAWGAFRHFLLEEDKPEEPTAHAFVSTLTRGDLSSIRWVCSSLRHAQPTCPG
AQLCTVYYASLNFRDIMLATGKLSPDAIPGKWTSQDSLLGMEFSGRDASGKRVMGLVPAK
GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGV
GQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDTSFEQHVLWHTGGKG
VDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFF
NESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQVLAEE
PEAVLKGAKPKLMSAISKTFCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGI
RTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLL
ENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSA
MERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLN
QPHMVLSSFVLAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSV
EVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLR
SLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLD
SIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGS
PTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAA
VDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGA
DYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVSVREG
Enzyme 1 Number of Residues 2511
Enzyme 1 Molecular Weight 273403
Enzyme 1 Theoretical pI 6.39
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • oxidoreductase activity
  • phosphopantetheine binding
  • transferase activity
  • vitamin binding
Process
  • biosynthesis
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid biosynthesis
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
—
Enzyme 1 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 1 Specific Function Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (3R)-3-hydroxypalmitoyl-[acyl-carrier protein] = 2-hexadecenoyl-[acyl-carrier protein] + H2O
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1049053 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P49327 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name FAS_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >7515 bp 
ATGGAGGAGGTGGTGATTGCCGGCATGTTCGGGAAGCTGCCAGAGTCGGAGAACTTGCAG
GAGTTCTGGGACAACCTCATCGGCGGTGTGGACATGGTCACGGACGATGACCGTCGCTGG
AAGGCTGGGCTCTACGGCCTGCCCCGGCGGTCCGGCAAGCTGAAGGACCTGTCTAGGTTT
GATGCCTCCTTCTTCGGAGTCCACCCCAAGCAGGCACACACGATGGACCCTCAGCTGCGG
CTGCTGCTGGAAGCTACCTATGAAGCCATCGTGGACGGAGGCATCAACCCAGATTCACTC
CGAGGAACACACACTGGCGTCTGGGTGGGCGTGAGCGGCTCTGAGACCTCGGAGGCCCTG
AGCCGAGACCCCGAGACACTCGTGGGCTACAGCATGGTGGGCTGCCAGCGAGCGATGATG
GCCAACCGGCTCTCCTTCTTCTTCGACTTCAGAGGGCCCAGCATCGCACTGGACACAGCC
TGCTCCTCCAGCCTGATGGCCCTGCAGAACGCCTACCAGGCCATCCACAGCGGGCAGTGC
CCTGCCGCCATCGTGGGGGGCATCAACGTCCTGCTGAAGCCCAACACCTCCGTGCAGTTC
TTGAGGCTGGGGATGCTCAGCCCCGAGGGCACCTGCAAGGCCTTCGACACAGCGGGGAAT
GGGTACTGCCGCTCGGAGGGTGTGGTGGCTGTCCTGCTGACCAAGAAGTCCCTGGCCCGG
AAGGTCTACACCACCATCCTGAACAAAGGCACCAATACAGATGGCTTCAAGGAGCAAGGC
GTGACCTTCCCTCAGGATATCCAGGAGCAGCCTATCCGCTCGTTGTACCAGTCGGCCGGA
GTGGCCCCTGAGTCATTTGAATACATCGAAGCCCACGGACCAGGCACCAAGGTGGGCGAC
CCCCAGGAGCGTAATGGCATCACCCGAGCCCTGTGCGCCACCCGCCAGGAGCCGCTGCTC
ATCGGCTCCACCAAGTCCAACATGGGGCACCCGGAGCCAGCCTCGGGGCTCGACGCCCTG
GCCAAGGTGCTGCTGTCCCTGGAGCACGGGCTCTGGGCCCCCAACCTGCACTTCCATAGC
CCCAACCCTGAGATCCCAGCGCTGTTGGATGGGCGGCTGCAGGTGGTGGACCAGCCCCTG
CCCGTCCGTGGCGGCAACGTGGGCATCAACTCCTTTGGCTTCGGGGGCTCCAACATGCAC
ATCATCCTGAGGCCCAACACGCAGTCCGCCCCCGCACCCGCCCCACATGCCACCCTGCCC
CGTCTGCTGCGGGCCAGCGGACGCACCCCTGAGGCCGTGCAGAAGCTGCTGGAGCAGGGC
CTCCGGCACAGCCAGGGCCTGGCTTTCCTGAGCATGCTGAACGACATCGCGGCTGTCCCC
GCCACCGCCATGCCCTTCCGTGGCTACGCTGTGCTGGGTGGTGAGACGCGGTGGCCCAGA
GTGCAGCAGGTGCCCGCTGGCGAGCGCCCGCTCTGGTTCATCTGCTCTGGGATGGGCACA
CAGTGGCGTGGAATGGGGCTGAGCCTTATGCGCCTGGACCGCTTCCGAGATTCCATCCTA
CGCTCCGATGAGGCTGTGAACCGATTCGGCCTGAAGGTGTCACAGCTGCTGCTGAGCACA
GACGAGAGCACCTTTGATGACATCGTCCATTCGTTTGTGAGCCTGACTGCCATCCAGATA
GGCCTCATAGACCTGCTGAGCTGCATGGGACCTGAGGCAGATGGCATCGTCGGCCACTCC
CTGGGGGAGTGGCTGTCGGTACGCGACGGCTGCCTGTCCCAGGAGGAGGCCGTCCTCGCT
GCCTACTGGAGGGGACAGTGCATCAAAGAAGCCCCACTTCCCGCCGGCGCCATGGCAGCC
GTGGGCTTGTCCTGGGAGGAGTGTAAACAGCGCTGCCCCCCTGCGGTGGTGCCCGCCTGC
CACAACTCCAAGGACACAGTCACCATCTCGGGACCTCAGGCCCCGGTGTTTGAGTTCGTG
GAGCAGCTGAGGAAGGAGGGTGTGTTTGCCAAGGAGGTGCGGACCGGCGGTATGGCCTTC
CACTCCTACTTCATGGAGGCCATCGCACCCCCACTGCTGCAGGAGCTCAAGAAGGTGATC
CGGGAGCCGAAGCCACGTTCAGCCCGCTGGCTCAGCACCTCTATCCCCGAGGCCCAGTGG
CACAGCAGCCTGGCACGCACGTCTTCCGCCGAGTACAATGTCAACAACCTGGTGAGCCCT
GTGCTGTTCCAGGAGGCCCTGTGGCACGTGCCTGAGCACGCGGTGGTGCTGGAGATCGCC
CCGACCCCGTGCCCTCAGGCTGTCCTGAAGCGGGTCCGTAAGCCGAGCTGCACCATCATC
CCCCGTATGAAGAAGGATCACAGGGACAACCTGGAGTTCTTCCTGGCCGGCATCGGCAGG
CTGCACCTCTCAGGCATCGACGCCAACCCCAATGCCTTGTTCCCACCTGTGGAGTCCCCA
GCTCCCCGAGGAACTCCCCTCATCTCCCCACTCATCAAGTGGGACCACAGCCTGGCCTGG
GACGCGCCGGCCGCCGAGGACTTCCCCAACGGTTCAGGTTCCCCCTCAGCCACCATCTAC
ACATGCACACCAAGCTCCGAGTCTCCTGACCGCTACCTGGTGGACCACACCATCGACGGT
CGCGTCCTCTTCCCCGCCACTGGCTACCTGAGCATAGTGTGGAAGACGCTGGCCCGCGCC
TGGGCTGGGCTCGAGCAGCTGCCTGTGGTGTTTGAGGATGTGGTGCAGCACCAGGCCACC
ATCCTGCCCAAGACTGGGACAGTGTCCTTGGAGGTACGGCTCCTGGAGGCCACCGGTGCC
TTCGAGGTGTCAGAGAACGGCAACCTGGTAGTGAGTGGGAAGGTGTACCAGTGGGATGAC
CCTGACCCCAGGCTCTTCGACCACCCGGAAAGTCCCCACCCCAATTCCCCACGGAGTCCC
CTCTTCCTGGCCCAGGCAGAAGTTTACAAGGAGCTGCGTCTGCGTGGCTACGACTACGGC
CCTCATTTCCAGGGCATCCTGGAGGCCAGCCTGGAAGGTGACTCGGGGAGGCTGCTGTGG
AAGGATAACTGGGTGAGCTTCATGGACACCATGCTGCAGATGTCCATCCTGGGCTCGGCC
AAGCACGGCCTGTACCTACCCACCCGTGTCACCGCCATCCACATCGACCCTGCCACCCAC
AGGCAGAAGCTGTACACACTGCAGGACAAGGCCCAAGTGGCTGACGTGGTGGTGAGCAGG
TGGCCGAGGGTCACAGTGGCGGGAGGCGTCCACATCTCCGGGCTCCACACTGAGTCGGCC
CCGCGGCGGCACGAGGAGCAGCAGGTGCCCATCCTGGAGAAGTTTTGCTTCACTCCCCAC
ACGGAGGAGGGGTGCCTGTCTGAGCACGCTGCCCTCGAGGAGGAGCTGCAACTGTGCAAG
GGGCTGGTCGAGGCACTCGAGACCAAGGTGACCCAGCAGGGGCTGAAGATGGTGGTGCCG
GACTGGACGGGGCCCAGATCCCCCCGGGACCCCTCACAGCAGGAACTGCCCCGGCTGTTG
TCGGCTGCCTGCAGGCTTCAGCTCAACGGGAACCTGCAGCTGGAGCTGGCGCAGGTGCTG
GCCCAGGAGAGGCCCAAGCTGCCAGAGGACCCTCTGCTCAGCGGCCTCCTGGACTCCCCG
GCACTCAAGGCCTGCCTGGACACTGCCGTGGAGAACATGCCCAGCCTGAAGATGAAGGTG
GTGGAGGTGCTGGCCGGCCACGGTCACCTGTATTCCCGCATCCCAGGCCTGCTCAGCCCC
CATCCCCTGCTGCAGCTGAGCTACACGGCCACCGACCGCCACCCCCAGGCCCTGGAGGCT
GCCCAGGCCGAGCTGCAGCAGCACGACGTTGCCCAGGGCCAGTGGGATCCCGCAGACCCT
GCCCCCAGCGCCCTGGGCAGCGCGGACCTCCTGGTGTGCAACTGTGCTGTGGCTGCCCTC
GGGGACCCGGCCTCAGCTCTCAGCAACATGGTGGCTGCCCTGAGAGAAGGGGGCTTTCTG
CTCCTGCACACACTGCTCCGGGGGCACCCTCGGGACATCGTGGCCTTCCTCACCTCCACT
GAGCCGCAGTATGGCCAGGGCATCCTGAGCCAGGACGCGTGGGAGAGCCTCTTCTCCAGG
GTGTCGCTGCGCCTGGTGGGCCTGAAGAAGTCCTTCTACGGCGCCACGCTCTTCCTGTGC
CGCCGGCCCACCCCGCAGGACAGCCCCATCTTCCTGCCGGTGGACGATACCAGCTTCCGC
TGGGTGGAGTCTCTGAAGGGCATCCTGGCTGACGAAGACTCTTCCCGGCCTGTGTGGCTG
AAGGCCATCAACTGTGCCACCTCGGGCGTGGTGGGCTTGGTGAACTGTCTCCGCCGAGAG
CCCGGCGGAACCGTCCGGTGTGTGCTGCTCTCCAACCTCAGCAGCACCTCCCACGTCCCG
GAGGTGGACCCGGGCTCCGCAGAACTGCAGAAGGTGTTGCAGGGAGACCTGGTGATGAAC
GTCTACCGCGACGGGGCCTGGGGGGTTTTCCGCCACTTCCTGCTGGAGGACAAGCCTGAG
GAGCCGACGGCACATGCCTTTGTGAGCACCCTCACCCGGGGGGACCTGTCCTCCATCCGC
TGGGTCTGCTCCTCGCTGCGCCATGCCCAGCCCACCTGCCCTGGCGCCCAGCTCTGCACG
GTCTACTACGCCTCCCTCAACTTCCGCGACATCATGCTGGCCACTGGCAAGCTGTCCCCT
GATGCCATCCCAGGGAAGTGGACCTCCCAGGACAGCCTGCTAGGTATGGAGTTCTCGGGC
CGAGACGCCAGCGGCAAGCGTGTGATGGGACTGGTGCCTGCCAAGGGCCTGGCCACCTCT
GTCCTGCTGTCACCGGACTTCCTCTGGGATGTGCCTTCCAACTGGACGCTGGAGGAGGCG
GCCTCGGTGCCTGTCGTCTACAGCACGGCCTACTACGCGCTGGTGGTGCGTGGGCGGGTG
CGCCCCGGGGAGACGCTGCTCATCCACTCGGGCTCGGGCGGCGTGGGCCAGGCCGCCATC
GCCATCGCCCTCAGTCTGGGCTGCCGCGTCTTCACCACCGTGGGGTCGGCTGAGAAGCGG
GCGTACCTCCAGGCCAGGTTCCCCCAGCTCGACAGCACCAGCTTCGCCAACTCCCGGGAC
ACATCCTTCGAGCAGCATGTGCTGTGGCACACGGGCGGGAAGGGCGTTGACCTGGTCTTG
AACTCCTTGGCGGAAGAGAAGCTGCAGGCCAGCGTGAGGTGCTTCGGTACGCACGGTCGC
TTCCTGGAAATTGGCAAATTCGACCTTTCTCAGAACCACCCGCTCGGCATGGCTATCTTC
CTGAAGAACGTGACATTCCACGGGGTCCTACTGGATGCGTTCTTCAACGAGAGCAGTGCT
GACTGGCGGGAGGTGTGGGCGCTTGTCGAGGCCGCCATCCGGGATGGGGTGGTACGGCCC
CTCAAGTGCACGGTGTTCCATGGGGCCCAGGTGGAGGACGCCTTCCGCTACATGGCCCAA
GGGAAGCACATTGGCAAAGTCGTCGTGCAGGTGCTTGCGGAGGAGCCGGCAGTGCTGAAG
GGGGCCAAACCCAAGCTGATGTCGGCCATCTCCAAGACCTTCTGCCCGGCCCACAAGAGC
TACATCATCGCTGGTGGTCTGGGTGGCTTCGGCCTGGAGTTGGCGCAGTGGCTGATACAG
CGTGGGGTGCAGAAGCTCGTGTTGACTTCTCGCTCCGGGATCCGGACAGGCTACCAGGCC
AAGCAGGTCCGCCGGTGGAGGCGCCAGGGGCTACAGGTGCAGGTGTCCACCAGCAACATC
AGCTCACTGGAGGGGGCCCGGGGCCTCATTGCCGAGGCGGCGCAGCTTGGGCCCGTGGGG
GGCGTCTTCAACCTGGCCGTGGTCTTGAGAGATGGCTTGCTGGAGAACCAGACCCCAGAG
TTCTTCCAGGACGTCTGCAAGCCCAAGTACAGCGGCACCCTGAACCTGGACAGGGTGACC
CGAGAGGCGTGCCCTGAGCTGGACTACTTTGTGGTCTTCTCCTCTGTGAGCTGCGGGCGT
GGCAATGCGGGACAGAGCAACTACGGCTTTGCCAATTCCGCCATGGAGCGTATCTGTGAG
AAACGCCGGCACGAAGGCCTCCCAGGCCTGGCCGTGCAGTGGGGCGCCATCGGCACCGTG
GGCATTTTGGTGGAGACGATGAGCACCAACGACACGATCGTCAGTGGCACGCTGCCCACG
CGCATTGGCGTCCTTGGCCTGGAGGTGCTGGACCTCTTCCTGAACCAGCCCCACATGGTC
CTGAGCAGCTTTGTGCTGGCTGAGAAGGCTGCGGCCTATAGGGACAGGGACAGCCAGCGG
GACCTGGTGGAGGCCGTGGCACACATCCTGGGCATCCGCGACTTGGCTGCTGTCAACCTG
GGCGGCTCACTGGCGGACCTGGGCCTGGACTCGCTCATGAGCGCGCCGGTGCGCCAGACG
CTGGAGCGTGAGCTCAACCTGGTGCTGTCCGTGCGCGAGGTGCGGCAACTCACGCTCCGG
AAACTGCAGGAGCTGTCCTCAAAGGCGGATGAAGCCAGCGAGCTGGCATGCCCCACGCCC
AAGGAGGATGGTCTGGCCCAGCAGCAGACTCAGCTGAACCTGCGCTCCCTGCTGGTGAAA
CCGGAGGGCCCCACCCTGATGCGGCTCAACTCCGTGCAGAGCTCGGAGCGGCCCCTGTTC
CTGGTGCACCCAATCGAGGCTACCACCGTGTTCCACAGCCTCGGTCCCGGTCTCAGCATC
CCCACCTATGGCCTGCAGTGCACCCCGGCTGCGCCCCTTGACAGCATCCACAGCCTGGCT
GCCTACTACATCGACTGCATCAGGCAGGTGCAGCCCGAGGGCCCCTACCGCGTGGCCGGC
TACTCCTACGGGGCCTGCGTGGCCTTTGAAATGTGCTCCCAGCTGCAGGCCCAGCAGAGC
CCAGCCCCCACCCACAACAGCCTCTTCCTGTTCGACGGCTCGCCCACCTACGTACTGGCC
TACACCCAGAGCTACCGGGCAAAGCTGACCCCAGGCTGTAAGGCTGAGGCTGAGACGGAG
GCCATATGCTTCTTCGTGCAGCAGTTCACGGACATGGAGCACAACAGGGTGCTGGAGGCG
CTGCTGCCGCTGAAGGGCCTAGAGGAGCGTGTGGCAGCCGCCGTGGACCTGATCATCAAG
AGCCACCAGGGCCTGGACCGCCAGGAGCTGAGCTTTGCGGCCCGGTCCTTCTACTACAGG
CTGCGTGCCGCTGACCAGTATACACCCAAGGCCAAGTACAGTGGCAACGTGATGCTACTG
CGGGCCAAGACGGGTGGCCGCTACGGCGAGGACCTGGGCGCGGACTACAACCTCTCCCAG
GTATGCGACGGGAAAGTATCCGTCCATATCATCGAGGGTGACCACCGCACGCTGCTGGAG
GGCAGCGGCCTGGAGTCCATCATCAGCATCATCCACAGCTCCCTGGCTGAGCCACGTGTG
AGTCGGGAGGGCTAG
Enzyme 1 GenBank Gene ID U26644 Link Image
Enzyme 1 GeneCard ID FASN Link Image
Enzyme 1 GenAtlas ID FASN Link Image
Enzyme 1 HGNC ID HGNC:3594 Link Image
Enzyme 1 Chromosome Location 17
Enzyme 1 Locus 17q25
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Jayakumar A, Tai MH, Huang WY, al-Feel W, Hsu M, Abu-Elheiga L, Chirala SS, Wakil SJ: Human fatty acid synthase: properties and molecular cloning. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8695-9. [PubMed Link Image]
  2. Kuhajda FP, Jenner K, Wood FD, Hennigar RA, Jacobs LB, Dick JD, Pasternack GR: Fatty acid synthesis: a potential selective target for antineoplastic therapy. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6379-83. [PubMed Link Image]
  3. Semenkovich CF, Coleman T, Fiedorek FT Jr: Human fatty acid synthase mRNA: tissue distribution, genetic mapping, and kinetics of decay after glucose deprivation. J Lipid Res. 1995 Jul;36(7):1507-21. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5351
Enzyme 2 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Enzyme 2 Synonyms
  1. E- NPP 1
  2. Phosphodiesterase I/nucleotide pyrophosphatase 1
  3. Plasma-cell membrane glycoprotein PC-1[Includes: Alkaline phosphodiesterase I
  4. NPPase]
Enzyme 2 Gene Name ENPP1
Enzyme 2 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 1 
MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED
Enzyme 2 Number of Residues 925
Enzyme 2 Molecular Weight 104925
Enzyme 2 Theoretical pI 7.14
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • endonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity
Enzyme 2 Pathways
Enzyme 2 Reactions
  • A dinucleotide + H2O = 2 mononucleotides
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 77-97
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 189650 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P22413 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ENPP1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2622 bp 
ATGGACGTGGGGGAGGAGCCGCTGGAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCC
AACACCTATAAAGTACTCTCGCTGGTATTGTCAGTATGTGTGTTAACAACAATACTTGGT
TGTATATTTGGGTTGAAACCAAGCTGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGT
TTCGAGAGAACATTTGGGAACTGTCGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGC
TGTTTAGATTACCAGGAGACGTGCATAGAACCAGAACATATATGGACTTGCAACAAATTC
AGGTGTGGTGAGAAAAGGTTGACCAGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGAC
AAGGGCGACTGCTGCATCAACTACAGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAA
GAACCATGTGAGAGCATTAATGAGCCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACC
CTCTTATTTTCTTTGGATGGATTCAGGGCAGAATATTTACACACTTGGGGTGGACTTCTT
CCTGTTATTAGCAAACTAAAAAAATGTGGAACATATACTAAAAACATGAGACCGGTATAT
CCAACAAAAACTTTCCCCAATCACTACAGCATTGTCACCGGATTGTATCCAGAATCTCAT
GGCATAATCGACAATAAAATGTATGATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGT
AAAGAGAAATTTAATCCTGAGTGGTACAAAGGAGAACCAATTTGGGTCACAGCTAAGTAT
CAAGGCCTCAAGTCTGGCACATTTTTCTGGCCAGGATCAGATGTGGAAATTAACGGAATT
TTCCCAGACATCTATAAAATGTATAATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCT
GTTCTTCAGTGGCTACAGCTTCCTAAAGATGAAAGACCACACTTTTACACTCTGTATTTA
GAAGAACCAGATTCTTCAGGTCATTCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCC
TTGCAGAGGGTTGATGGTATGGTTGGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTG
CACAGATGCCTGAACCTCATCCTTATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAG
AAATACATATATCTGAATAAATATTTGGGGGATGTTAAAAATATTAAAGTTATCTATGGA
CCTGCAGCTCGATTGAGACCCTCTGATGTCCCAGATAAATACTATTCATTTAACTATGAA
GGCATTGCCCGAAATCTTTCTTGCCGGGAACCAAACCAGCACTTCAAACCTTACCTGAAA
CATTTCTTACCTAAGCGTTTGCACTTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTC
TATTTGGACCCTCAGTGGCAACTTGCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGT
GGATTTCATGGCTCTGACAATGTATTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGA
CCTGGATTCAAGCATGGCATTGAGGCTGACACCTTTGAAAACATTGAAGTCTATAACTTA
ATGTGTGATTTACTGAATTTGACACCGGCTCCTAATAACGGAACTCATGGAAGTCTTAAC
CACCTTCTAAAGAATCCTGTTTATACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTA
CAGTGCCCCTTCACAAGAAACCCCAGAGATAACCTTGGCTGCTCATGTAACCCTTCGATT
TTGCCGATTGAGGATTTTCAAACACAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATT
AAGCATGAAACTTTACCCTATGGAAGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGT
CTTCTTTCCCAGCACCAGTTTATGAGTGGATACAGCCAAGACATCTTAATGCCCCTTTGG
ACATCCTATACCGTGGACAGAAATGACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTG
TACCAGGACTTTAGAATTCCTCTTAGTCCTGTCCATAAATGTTCATTTTATAAAAATAAC
ACCAAAGTGAGTTACGGGTTCCTCTCCCCACCACAACTAAATAAAAATTCAAGTGGAATA
TATTCTGAAGCTTTGCTTACTACAAATATAGTGCCAATGTACCAGAGTTTTCAAGTTATA
TGGCGCTACTTTCATGACACCCTACTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAAT
GTCGTCAGTGGTCCTGTGTTTGACTTTGATTATGATGGACGTTGTGATTCCTTAGAGAAT
CTGAGGCAAAAAAGAAGAGTCATCCGTAACCAAGAAATTTTGATTCCAACTCACTTCTTT
ATTGTGCTAACAAGCTGTAAAGATACATCTCAGACGCCTTTGCACTGTGAAAACCTAGAC
ACCTTAGCTTTCATTTTGCCTCACAGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAG
CATGACTCCTCATGGGTTGAAGAATTGTTAATGTTACACAGAGCACGGATCACAGATGTT
GAGCACATCACTGGACTCAGCTTCTATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTA
AAGTTGAAAACACATTTGCCAACCTTTAGCCAAGAAGACTGA
Enzyme 2 GenBank Gene ID M57736 Link Image
Enzyme 2 GeneCard ID ENPP1 Link Image
Enzyme 2 GenAtlas ID ENPP1 Link Image
Enzyme 2 HGNC ID HGNC:3356 Link Image
Enzyme 2 Chromosome Location 6
Enzyme 2 Locus 6q22-q23
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed Link Image]
  2. Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed Link Image]
  5. Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed Link Image]
  6. Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed Link Image]
  7. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed Link Image]
  8. Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5406
Enzyme 3 Name Acyl carrier protein, mitochondrial precursor
Enzyme 3 Synonyms
  1. ACP
  2. NADH-ubiquinone oxidoreductase 9.6 kDa subunit
  3. CI-SDAP
Enzyme 3 Gene Name NDUFAB1
Enzyme 3 Protein Sequence >Acyl carrier protein, mitochondrial precursor 
MASRVLSAYVSRLPAAFAPLPRVRMLAVARPLSTALCSAGTQTRLGTLQPALVLAQVPGR
VTQLCRQYSDMPPLTLEGIQDRVLYVLKLYDKIDPEKLSVNSHFMKDLGLDSLDQVEIIM
AMEDEFGFEIPDIDAEKLMCPQEIVDYIADKKDVYE
Enzyme 3 Number of Residues 156
Enzyme 3 Molecular Weight 17418
Enzyme 3 Theoretical pI 4.53
Enzyme 3 GO Classification
Function
  • acyl carrier activity
  • binding
  • carrier activity
  • cofactor binding
  • phosphopantetheine binding
  • transporter activity
  • vitamin binding
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid biosynthesis
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
—
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function Carrier of the growing fatty acid chain in fatty acid biosynthesis in mitochondria
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-29
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 4567042 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O14561 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ACPM_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >471 bp 
ATGGCGTCTCGTGTCCTTTCAGCCTATGTCAGCCGCCTGCCCGCGGCCTTTGCGCCGCTG
CCCCGGGTCCGGATGCTGGCCGTGGCCCGGCCTCTCAGCACTGCTCTCTGCTCCGCGGGG
ACCCAGACGAGGCTCGGGACTTTGCAGCCGGCCTTAGTGCTCGCGCAGGTTCCTGGTAGA
GTTACACAGTTGTGCCGCCAGTATAGCGACATGCCTCCTTTGACGTTAGAGGGCATCCAG
GACCGTGTTCTTTACGTATTGAAACTCTATGACAAGATTGACCCAGAGAAGCTTTCAGTA
AATTCTCATTTTATGAAAGACCTGGGCTTAGACAGTTTGGACCAAGTGGAGATTATCATG
GCCATGGAAGACGAATTTGGGTTTGAAATTCCTGATATAGATGCTGAAAAGTTAATGTGT
CCACAAGAAATTGTAGATTACATTGCAGATAAGAAAGATGTATATGAATAA
Enzyme 3 GenBank Gene ID AF087660 Link Image
Enzyme 3 GeneCard ID NDUFAB1 Link Image
Enzyme 3 GenAtlas ID NDUFAB1 Link Image
Enzyme 3 HGNC ID HGNC:7694 Link Image
Enzyme 3 Chromosome Location 16
Enzyme 3 Locus 16p12.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA: cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. Biochem Biophys Res Commun. 1998 Dec 18;253(2):415-22. [PubMed Link Image]
  2. Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J, Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y, Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC, Adams MD: Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. Genomics. 1999 Sep 15;60(3):295-308. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5426
Enzyme 4 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
Enzyme 4 Synonyms
  1. E- NPP 3
  2. Phosphodiesterase I/nucleotide pyrophosphatase 3
  3. Phosphodiesterase I beta
  4. PD-Ibeta
  5. CD203c antigen[Includes: Alkaline phosphodiesterase I
  6. NPPase]
Enzyme 4 Gene Name ENPP3
Enzyme 4 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 3 
MESTLTLATEQPVKKNTLKKYKIACIVLLALLVIMSLGLGLGLGLRKLEKQGSCRKKCFD
ASFRGLENCRCDVACKDRGDCCWDFEDTCVESTRIWMCNKFRCGETRLEASLCSCSDDCL
QKKDCCADYKSVCQGETSWLEENCDTAQQSQCPEGFDLPPVILFSMDGFRAEYLYTWDTL
MPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVNLNKNFSLS
SKEQNNPAWWHGQPMWLTAMYQGLKAATYFWPGSEVAINGSFPSIYMPYNGSVPFEERIS
TLLKWLDLPKAERPRFYTMYFEEPDSSGHAGGPVSARVIKALQVVDHAFGMLMEGLKQRN
LHNCVNIILLADHGMDQTYCNKMEYMTDYFPRINFFYMYEGPAPRIRAHNIPHDFFSFNS
EEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKVHLFVDQQWLAVRSKSNTNCGG
GNHGYNNEFRSMEAIFLAHGPSFKEKTEVEPFENIEVYNLMCDLLRIQPAPNNGTHGSLN
HLLKVPFYEPSHAEEVSKFSVCGFANPLPTESLDCFCPHLQNSTQLEQVNQMLNLTQEEI
TATVKVNLPFGRPRVLQKNVDHCLLYHREYVSGFGKAMRMPMWSSYTVPQLGDTSPLPPT
VPDCLRADVRVPPSESQKCSFYLADKNITHGFLYPPASNRTSDSQYDALITSNLVPMYEE
FRKMWDYFHSVLLIKHATERNGVNVVSGPIFDYNYDGHFDAPDEITKHLANTDVPIPTHY
FVVLTSCKNKSHTPENCPGWLDVLPFIIPHRPTNVESCPEGKPEALWVEERFTAHIARVR
DVELLTGLDFYQDKVQPVSEILQLKTYLPTFETTI
Enzyme 4 Number of Residues 875
Enzyme 4 Molecular Weight 100097
Enzyme 4 Theoretical pI 6.55
Enzyme 4 GO Classification
Function
  • binding
  • catalytic activity
  • endonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
—
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD
Enzyme 4 Pathways
Enzyme 4 Reactions
  • A dinucleotide + H2O = 2 mononucleotides
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-38
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 2465540 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O14638 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name ENPP3_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2628 bp 
ATGGAATCTACGTTGACTTTAGCAACGGAACAACCTGTTAAGAAGAACACTCTTAAGAAA
TATAAAATAGCTTGCATTGTTCTTCTTGCTTTGCTGGTGATCATGTCACTTGGATTAGGC
CTGGGGCTTGGACTCAGGAAACTGGAAAAGCAAGGCAGCTGCAGGAAGAAGTGCTTTGAT
GCATCATTTAGAGGACTGGAGAACTGCCGGTGTGATGTGGCATGTAAAGACCGAGGTGAT
TGCTGCTGGGATTTTGAAGACACCTGTGTGGAATCAACTCGAATATGGATGTGCAATAAA
TTTCGTTGTGGAGAGACCAGATTAGAGGCCAGCCTTTGCTCTTGTTCAGATGACTGTTTG
CAGAAGAAAGATTGCTGTGCTGACTATAAGAGTGTTTGCCAAGGAGAAACCTCATGGCTG
GAAGAAAACTGTGACACAGCCCAGCAGTCTCAGTGCCCAGAAGGGTTTGACCTGCCACCA
GTTATCTTGTTTTCTATGGATGGATTTAGAGCTGAATATTTATACACATGGGATACTTTA
ATGCCAAATATCAATAAACTGAAAACATGTGGAATTCATTCAAAATACATGAGAGCTATG
TATCCTACCAAAACCTTCCCAAATCATTACACCATTGTCACGGGCTTGTATCCAGAGTCA
CATGGCATCATTGACAATAATATGTATGATGTAAATCTCAACAAGAATTTTTCACTTTCT
TCAAAGGAACAAAATAATCCAGCCTGGTGGCATGGGCAACCAATGTGGCTGACAGCAATG
TATCAAGGTTTAAAAGCCGCTACCTACTTTTGGCCCGGATCAGAAGTGGCTATAAATGGC
TCCTTTCCTTCCATATACATGCCTTACAACGGAAGTGTCCCATTTGAAGAGAGGATTTCT
ACACTGTTAAAATGGCTGGACCTGCCCAAAGCTGAAAGACCCAGGTTTTATACCATGTAT
TTTGAAGAACCTGATTCCTCTGGACATGCAGGTGGACCAGTCAGTGCCAGAGTAATTAAA
GCCTTACAGGTAGTAGATCATGCTTTTGGGATGTTGATGGAAGGCCTGAAGCAGCGGAAT
TTGCACAACTGTGTCAATATCATCCTTCTGGCTGACCATGGAATGGACCAGACTTATTGT
AACAAGATGGAATACATGACTGATTATTTTCCCAGAATAAACTTCTTCTACATGTACGAA
GGGCCTGCCCCCCGCATCCGAGCTCATAATATACCTCATGACTTTTTTAGTTTTAATTCT
GAGGAAATTGTTAGAAACCTCAGTTGCCGAAAACCTGATCAGCATTTCAAGCCCTATTTG
ACTCCTGATTTGCCAAAGCGACTGCACTATGCCAAGAACGTCAGAATCGACAAAGTTCAT
CTCTTTGTGGATCAACAGTGGCTGGCTGTTAGGAGTAAATCAAATACAAATTGTGGAGGA
GGCAACCATGGTTATAACAATGAGTTTAGGAGCATGGAGGCTATCTTTCTGGCACATGGA
CCCAGTTTTAAAGAGAAGACTGAAGTTGAACCATTTGAAAATATTGAAGTCTATAACCTA
ATGTGTGATCTTCTACGCATTCAACCAGCACCAAACAATGGAACCCATGGTAGTTTAAAC
CATCTTCTGAAGGTGCCTTTTTATGAGCCATCCCATGCAGAGGAGGTGTCAAAGTTTTCT
GTTTGTGGCTTTGCTAATCCATTGCCCACAGAGTCTCTTGACTGTTTCTGCCCTCACCTA
CAAAATAGTACTCAGCTGGAACAAGTGAATCAGATGCTAAATCTCACCCAAGAAGAAATA
ACAGCAACAGTGAAAGTAAATTTGCCATTTGGGAGGCCTAGGGTACTGCAGAAGAACGTG
GACCACTGTCTCCTTTACCACAGGGAATATGTCAGTGGATTTGGAAAAGCTATGAGGATG
CCCATGTGGAGTTCATACACAGTCCCCCAGTTGGGAGACACATCGCCTCTGCCTCCCACT
GTCCCAGACTGTCTGCGGGCTGATGTCAGGGTTCCTCCTTCTGAGAGCCAAAAATGTTCC
TTCTATTTAGCAGACAAGAATATCACCCACGGCTTCCTCTATCCTCCTGCCAGCAATAGA
ACATCAGATAGCCAATATGATGCTTTAATTACTAGCAATTTGGTACCTATGTATGAAGAA
TTCAGAAAAATGTGGGACTACTTCCACAGTGTTCTTCTTATAAAACATGCCACAGAAAGA
AATGGAGTAAATGTGGTTAGTGGACCAATATTTGATTATAATTATGATGGCCATTTTGAT
GCTCCAGATGAAATTACCAAACATTTAGCCAACACTGATGTTCCCATCCCAACACACTAC
TTTGTGGTGCTGACCAGTTGTAAAAACAAGAGCCACACACCGGAAAACTGCCCTGGGTGG
CTGGATGTCCTACCCTTTATCATCCCTCACCGACCTACCAACGTGGAGAGCTGTCCTGAA
GGTAAACCAGAAGCTCTTTGGGTTGAAGAAAGATTTACAGCTCACATTGCCCGGGTCCGT
GATGTAGAACTTCTCACTGGGCTTGACTTCTATCAGGATAAAGTGCAGCCTGTCTCTGAA
ATTTTGCAACTAAAGACATATTTACCAACATTTGAAACCACTATTTAA
Enzyme 4 GenBank Gene ID AF005632 Link Image
Enzyme 4 GeneCard ID ENPP3 Link Image
Enzyme 4 GenAtlas ID ENPP3 Link Image
Enzyme 4 HGNC ID HGNC:3358 Link Image
Enzyme 4 Chromosome Location 6
Enzyme 4 Locus 6q22
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6312
Enzyme 5 Name Pantothenate kinase 4
Enzyme 5 Synonyms
  1. Pantothenic acid kinase 4
  2. hPanK4
Enzyme 5 Gene Name PANK4
Enzyme 5 Protein Sequence >Pantothenate kinase 4 
MAECGASGSGSSGDSLDKSITLPPDEIFRNLENAKRFAIDIGGSLTKLAYYSTVQHKVAK
VRSFDHSGKDTEREHEPPYEISVQEEITARLHFIKFENTYIEACLDFIKDHLVNTETKVI
QATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFVYQKDSDPEFRFQ
TNHPHIFPYLLVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLH
LASRGQHSNVDMLVRDVYGGAHQTLGLSGNLIASSFGKSATADQEFSKEDMAKSLLHMIS
NDIGQLACLHARLHSLDRVYFGGFFIRGHPVTMRTITYSINFFSKGEVQALFLRHEGYLG
AIGAFLKGAEQDNPNQYSWGENYAGSSGLMSASPELGPAQRARSGTFDLLEMDRLERPLV
DLPLLLDPPSYVPDTVDLTDDALARKYWLTCFEEALDGVVKRAVASQPDSVDAAERAEKF
RQKYWNKLQTLRQQPFAYGTLTVRSLLDTREHCLNEFNFPDPYSKVKQRENGVALRCFPG
VVRSLDALGWEERQLALVKGLLAGNVFDWGAKAVSAVLESDPYFGFEEAKRKLQERPWLV
DSYSEWLQRLKGPPHKCALIFADNSGIDIILGVFPFVRELLLRGTEVILACNSGPALNDV
THSESLIVAERIAGMDPVVHSALQEERLLLVQTGSSSPCLDLSRLDKGLAALVRERGADL
VVIEGMGRAVHTNYHAALRCESLKLAVIKNAWLAERLGGRLFSVIFKYEVPAE
Enzyme 5 Number of Residues 773
Enzyme 5 Molecular Weight 85992
Enzyme 5 Theoretical pI 6.22
Enzyme 5 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • pantothenate kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • coenzyme A biosynthesis
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Plays a role in the physiological regulation of the intracellular CoA concentration
Enzyme 5 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
Enzyme 5 Reactions
  • ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 7023024 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9NVE7 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PANK4_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2322 bp 
ATGGCGGAGTGTGGAGCGAGCGGCAGCGGGAGCAGCGGGGACAGTCTGGACAAGAGCATC
ACGCTGCCCCCCGACGAGATCTTCCGCAACCTGGAGAACGCCAAGCGCTTCGCCATCGAC
ATAGGCGGGTCGTTAACCAAGCTGGCCTACTATTCAACGGTACAGCACAAAGTCGCCAAG
GTGCGGTCTTTCGACCACTCCGGAAAGGACACAGAACGTGAACATGAGCCGCCCTATGAG
ATTTCAGTTCAAGAAGAGATCACTGCTCGACTGCACTTCATTAAGTTTGAGAATACCTAC
ATCGAAGCCTGCCTGGACTTCATCAAAGACCATCTCGTCAACACAGAGACCAAGGTCATC
CAGGCGACCGGGGGCGGGGCCTACAAGTTCAAGGACCTCATCGAAGAGAAGCTGCGGCTG
AAAGTCGACAAGGAGGACGTGATGACGTGCCTGATTAAGGGGTGCAACTTCGTGCTCAAG
AACATCCCCCATGAGGCCTTCGTGTACCAGAAGGATTCCGACCCTGAGTTCCGGTTCCAG
ACCAACCACCCCCACATTTTCCCCTATCTTCTTGTCAATATCGGCTCTGGAGTCTCCATC
GTGAAGGTGGAGACGGAGGACAGGTTCGAGTGGGTCGGCGGCAGCTCCATTGGAGGCGGC
ACCTTCTGGGGGCTTGGCGCTCTGCTCACCAAAACGAAGAAGTTTGACGAGCTCCTGCAC
CTGGCCTCGAGGGGCCAGCACAGCAATGTGGACATGCTGGTGCGGGACGTCTACGGCGGC
GCCCACCAGACTCTCGGGCTGAGCGGGAACCTCATCGCCAGCAGCTTCGGGAAGTCGGCC
ACCGCCGACCAAGAGTTCTCCAAAGAAGACATGGCGAAGAGCCTGCTGCACATGATCAGC
AACGACATTGGGCAGCTGGCCTGCCTCCACGCACGGCTGCACAGCCTGGACCGCGTGTAC
TTTGGAGGCTTCTTTATCCGGGGCCACCCCGTGACCATGCGCACCATCACCTATAGCATC
AACTTCTTCTCCAAGGGGGAAGTGCAGGCGCTGTTTCTGAGGCACGAAGGCTACCTGGGA
GCCATCGGAGCGTTCCTGAAAGGAGCTGAGCAGGACAATCCTAACCAGTACAGCTGGGGA
GAGAACTATGCAGGCAGCTCCGGGCTGATGAGTGCATCACCCGAGCTCGGCCCGGCGCAG
CGGGCGCGGAGTGGCACTTTTGACTTGCTGGAAATGGACCGGCTGGAGAGGCCACTGGTT
GACCTGCCGCTCCTCCTGGACCCGCCCTCCTACGTGCCCGACACGGTGGACCTCACCGAT
GACGCTCTGGCCCGAAAATACTGGCTCACCTGCTTTGAGGAGGCCCTGGACGGGGTAGTG
AAGCGCGCAGTGGCGAGCCAGCCAGACTCTGTGGATGCAGCCGAGAGGGCGGAGAAGTTC
CGGCAGAAGTACTGGAACAAGCTTCAGACCCTGAGGCAGCAGCCCTTCGCCTATGGGACC
CTGACCGTGCGCAGCCTGCTGGACACCAGGGAGCACTGTCTGAACGAGTTCAACTTCCCG
GATCCCTACTCCAAAGTGAAGCAGCGGGAGAATGGCGTGGCGCTGAGGTGCTTCCCCGGG
GTCGTGCGCTCCCTGGACGCGCTGGGCTGGGAGGAACGGCAGCTGGCGCTGGTGAAAGGC
CTCCTGGCGGGGAATGTCTTCGACTGGGGGGCCAAAGCCGTGTCTGCTGTCCTTGAATCC
GACCCCTACTTTGGGTTTGAAGAAGCAAAGAGGAAGTTACAAGAAAGACCCTGGCTCGTG
GATTCCTACAGCGAGTGGCTTCAGAGATTAAAGGGGCCCCCTCATAAATGTGCCTTAATT
TTCGCAGATAACAGTGGAATAGACATCATTTTGGGAGTCTTCCCCTTTGTCAGGGAGCTA
CTCCTTAGAGGGACAGAGGTCATCCTGGCGTGCAACTCAGGCCCCGCCCTGAACGACGTG
ACCCACAGCGAGTCCCTCATCGTGGCAGAGCGTATTGCGGGCATGGACCCTGTCGTGCAC
TCTGCGCTCCAGGAAGAGAGGCTGCTGCTGGTGCAGACGGGCTCCAGCTCCCCGTGCCTC
GACCTCAGCCGCCTGGATAAGGGGCTGGCCGCACTGGTGCGGGAGCGTGGCGCGGATCTG
GTGGTCATCGAGGGCATGGGCCGTGCTGTCCACACAAACTACCACGCAGCCCTGCGCTGC
GAGAGCCTCAAGCTGGCCGTCATCAAGAACGCGTGGCTGGCCGAGCGGCTGGGCGGCCGG
CTCTTCAGCGTCATCTTCAAGTACGAGGTCCCAGCCGAGTGA
Enzyme 5 GenBank Gene ID AK001644 Link Image
Enzyme 5 GeneCard ID PANK4 Link Image
Enzyme 5 GenAtlas ID PANK4 Link Image
Enzyme 5 HGNC ID HGNC:19366 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 1p36.32
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Zhou B, Westaway SK, Levinson B, Johnson MA, Gitschier J, Hayflick SJ: A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome. Nat Genet. 2001 Aug;28(4):345-9. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6314
Enzyme 6 Name Pantothenate kinase 1
Enzyme 6 Synonyms
  1. Pantothenic acid kinase 1
  2. hPanK1
  3. hPanK
Enzyme 6 Gene Name PANK1
Enzyme 6 Protein Sequence >Pantothenate kinase 1 
MLKLVGGGGGQDWACSVAGTSLGGEEAAFEVARPGDQGKAGGGSPGWGCAGIPDSAPGAG
VLQAGAVGPARGGQGAEEVGESAGGGEERRVRHPQAPALRLLNRKPQGGSGEIKTPENDL
QRGRLSRGPRTAPPAPGMGDRSGQQERSVPHSPGAPVGTSAAAVNGLLHNGFHPPPVQPP
HVCSRGPVGGSDAAPQRLPLLPELQPQPLLPQHDSPAKKCRLRRRMDSGRKNRPPFPWFG
MDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTM
CGRKGNLHFIRFPSCAMHRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHK
LDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELCQKKPYCLDNPYPMLLVNMGSGVS
ILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKDIYG
GDYERFGLQGSAVASSFGNMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENID
RVVFVGNFLRINMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALLELFKMTDDK
Enzyme 6 Number of Residues 598
Enzyme 6 Molecular Weight 64340
Enzyme 6 Theoretical pI 7.61
Enzyme 6 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • pantothenate kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • coenzyme A biosynthesis
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Plays a role in the physiological regulation of the intracellular CoA concentration
Enzyme 6 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
Enzyme 6 Reactions
  • ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 19223870 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q8TE04 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PANK1_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >945 bp 
ATGAAGCTTATAAATGGCAAAAAGCAAACATTCCCATGGTTTGGCATGGACATCGGTGGA
ACGCTGGTTAAATTGGTGTATTTCGAGCCGAAGGATATTACAGCCGAAGAGGAGCAAGAG
GAAGTGGAGAACCTGAAGAGCATCCGGAAGTATTTGACTTCTAATACTGCTTATGGGAAA
ACTGGGATCCGAGACGTCCACCTGGAACTGAAAAACCTGACCATGTGTGGACGCAAAGGG
GACCTGCACTTCATCCGCTTTCCCAGCTGTGCTATGCACAGGTTCATTCAGATGGGCAGC
GAGAAGAACTTCTCTAGCCTTCACACCACCCTCTGCGCCACAGGAGGCGGGGCTTTCAAA
TTCGAAGAGGACTTCAGAATGATTGCTGACCTGCAGCTGCATAAACTGGATGAACTGGAC
TGTCTGATTCAGGGCCTGCTTTATGTCGACTCTGTTGGCTTCAACGGCAAGCCAGAATGT
TACTATTTTGAAAATCCCACAAATCCTGAATTGTGTCAAAAAAAGCCGTACTGCCTTGAT
AACCCATACCCTATGTTGCTGGTTAACATGGGCTCAGGTGTCAGCATTCTAGCCGTGTAC
TCCAAGGACAACTATAAAAGAGTTACAGGGACCAGCTTTGGCAACATGATGAGTAAAGAA
AAGCGAGATTCCATCAGCAAGGAAGACCTCGCCCGGGCCACATTGGTCACCATCACCAAC
AACATTGGCTCCATTGCTCGGATGTGTGCGTTGAATGAGAACATAGACAGAGTTGTGTTT
GTTGGAAATTTTCTCAGAATCAATATGGTCTCCATGAAGCTGCTGGCATATGCCATGGAT
TTTTGGTCCAAAGGACAACTGAAAGCTCTGTTTTTGGAACATGAGGGTTATTTTGGAGCC
GTTGGGGCACTGTTGGAACTGTTCAAAATGACTGATGACAAGTAG
Enzyme 6 GenBank Gene ID AF355198 Link Image
Enzyme 6 GeneCard ID PANK1 Link Image
Enzyme 6 GenAtlas ID PANK1 Link Image
Enzyme 6 HGNC ID HGNC:8598 Link Image
Enzyme 6 Chromosome Location 10
Enzyme 6 Locus 10q23.31
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Ni X, Ma Y, Cheng H, Jiang M, Ying K, Xie Y, Mao Y: Cloning and characterization of a novel human pantothenate kinase gene. Int J Biochem Cell Biol. 2002 Feb;34(2):109-15. [PubMed Link Image]
  2. Zhou B, Westaway SK, Levinson B, Johnson MA, Gitschier J, Hayflick SJ: A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome. Nat Genet. 2001 Aug;28(4):345-9. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6315
Enzyme 7 Name Pantothenate kinase 3
Enzyme 7 Synonyms
  1. Pantothenic acid kinase 3
  2. hPanK3
Enzyme 7 Gene Name PANK3
Enzyme 7 Protein Sequence >Pantothenate kinase 3 
MKIKDAKKPSFPWFGMDIGGTLVKLSYFEPIDITAEEEQEEVESLKSIRKYLTSNVAYGS
TGIRDVHLELKDLTLFGRRGNLHFIRFPTQDLPTFIQMGRDKNFSTLQTVLCATGGGAYK
FEKDFRTIGNLHLHKLDELDCLVKGLLYIDSVSFNGQAECYYFANASEPERCQKMPFNLD
DPYPLLVVNIGSGVSILAVHSKDNYKRVTGTSLGGGTFLGLCSLLTGCESFEEALEMASK
GDSTQADKLVRDIYGGDYERFGLPGWAVASSFGNMIYKEKRESVSKEDLARATLVTITNN
IGSVARMCAVNEKINRVVFVGNFLRVNTLSMKLLAYALDYWSKGQLKALFLEHEGYFGAV
GALLGLPNFS
Enzyme 7 Number of Residues 370
Enzyme 7 Molecular Weight 41095
Enzyme 7 Theoretical pI 6.52
Enzyme 7 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • pantothenate kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • coenzyme A biosynthesis
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Plays a role in the physiological regulation of the intracellular CoA concentration
Enzyme 7 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
Enzyme 7 Reactions
  • ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 10434655 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9H999 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PANK3_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1113 bp 
ATGAAGATCAAAGATGCCAAGAAACCCTCTTTCCCATGGTTTGGCATGGACATTGGGGGA
ACTCTAGTAAAGCTCTCGTACTTTGAACCTATTGATATCACAGCAGAGGAAGAGCAAGAA
GAAGTTGAGAGTTTAAAAAGTATTCGGAAATATTTGACTTCTAACGTGGCATATGGATCC
ACCGGCATTCGGGATGTACACCTTGAACTGAAAGATTTAACACTTTTTGGCCGAAGAGGG
AACTTGCACTTTATCAGGTTTCCAACCCAGGACCTGCCTACTTTTATCCAAATGGGAAGA
GATAAAAACTTCTCAACATTGCAGACGGTGCTATGTGCTACAGGAGGTGGTGCTTACAAG
TTTGAAAAAGATTTTCGCACAATTGGAAACCTCCACCTGCACAAACTGGATGAACTTGAC
TGCCTTGTAAAGGGCTTGCTGTATATAGACTCTGTCAGTTTCAATGGACAAGCCGAGTGC
TATTATTTTGCTAATGCCTCAGAACCTGAGCGATGCCAAAAGATGCCTTTTAACCTGGAT
GATCCCTATCCACTGCTTGTAGTGAACATTGGCTCAGGAGTCAGTATTTTAGCAGTCCAT
TCCAAAGACAACTATAAACGAGTGACTGGGACAAGCCTTGGAGGGGGTACCTTTCTGGGT
TTATGCAGTTTATTGACTGGCTGTGAAAGTTTTGAAGAGGCTCTTGAAATGGCATCCAAA
GGTGATAGCACACAAGCTGACAAGCTGGTCCGTGATATTTATGGAGGAGATTATGAAAGA
TTTGGTTTGCCAGGTTGGGCTGTAGCATCTAGTTTTGGGAATATGATTTATAAGGAGAAG
CGAGAATCTGTTAGTAAAGAAGATCTGGCAAGAGCTACTTTAGTTACTATCACCAATAAC
ATTGGTTCTGTGGCACGAATGTGTGCTGTTAATGAGAAAATAAACAGAGTTGTCTTTGTT
GGAAACTTTTTACGTGTCAATACCCTCTCAATGAAACTTTTGGCATATGCACTGGATTAC
TGGTCAAAAGGTCAACTAAAAGCATTGTTTCTAGAACATGAGGGTTACTTTGGAGCAGTT
GGTGCACTTCTTGGGCTGCCAAATTTCAGCTAA
Enzyme 7 GenBank Gene ID AK022961 Link Image
Enzyme 7 GeneCard ID PANK3 Link Image
Enzyme 7 GenAtlas ID PANK3 Link Image
Enzyme 7 HGNC ID HGNC:19365 Link Image
Enzyme 7 Chromosome Location 5
Enzyme 7 Locus 5q34
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Zhou B, Westaway SK, Levinson B, Johnson MA, Gitschier J, Hayflick SJ: A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome. Nat Genet. 2001 Aug;28(4):345-9. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 7284
Enzyme 8 Name Bifunctional coenzyme A synthase
Enzyme 8 Synonyms
  1. CoA synthase
  2. NBP
  3. POV-2[Includes: Phosphopantetheine adenylyltransferase
  4. Pantetheine-phosphate adenylyltransferase
  5. PPAT
  6. Dephospho-CoA pyrophosphorylase
  7. Dephospho-CoA kinase
  8. DPCK
  9. Dephosphocoenzyme A kinase
  10. DPCOAK]
Enzyme 8 Gene Name COASY
Enzyme 8 Protein Sequence >Bifunctional coenzyme A synthase 
MAVFRSGLLVLTTPLASLAPRLASILTSAARLVNHTLYVHLQPGMSLEGPAQPQSSPVQA
TFEVLDFITHLYAGADVHRHLDVRILLTNIRTKSTFLPPLPTSVQNLAHPPEVVLTDFQT
LDGSQYNPVKQQLVRYATSCYSCCPRLASVLLYSDYGIGEVPVEPLDVPLPSTIRPASPV
AGSPKQPVRGYYRGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPEL
LQPYTERVEHLSEFLVDIKPSLTFDVIPLLDPYGPAGSDPSLEFLVVSEETYRGGMAINR
FRLENDLEELALYQIQLLKDLRHTENEEDKVSSSSFRQRMLGNLLRPPYERPELPTCLYV
IGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGI
INRKVLGSRVFGNKKQLKILTDIMWPIIAKLAREEMDRAVAEGKRVCVIDAAVLLEAGWQ
NLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQMSGQQLVEQSHVVLSTLWEPHI
TQRQVEKAWALLQKRIPKTHQALD
Enzyme 8 Number of Residues 564
Enzyme 8 Molecular Weight 62330
Enzyme 8 Theoretical pI 6.99
Enzyme 8 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleotide binding
  • nucleotidyltransferase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
—
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopantetheine adenylyltransferase, coded by the coaD domain; the fifth reaction is catalyzed by the dephospho-CoA kinase, coded by the coaE domain. May act as a point of CoA biosynthesis regulation
Enzyme 8 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
Enzyme 8 Reactions
  • ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-23
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 17981025 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q13057 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name COASY_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1695 bp 
ATGGCCGTATTCCGGTCGGGTCTCCTGGTGCTGACGACGCCGCTGGCCTCCCTAGCCCCT
CGCCTGGCCTCCATCCTGACCTCGGCGGCCCGGCTGGTGAATCACACACTCTATGTTCAC
CTGCAGCCGGGCATGAGCCTGGAGGGCCCGGCTCAGCCCCAGTACAGCCCCGTGCAGGCC
ACGTTTGAGGTTCTTGATTTCATCACGCACCTCTATGCTGGCGCCGACGTCCACAGGCAC
TTGGACGTCAGAATCCTACTGACCAATATCCGAACCAAGAGCACCTTTCTCCCTCCCCTG
CCCACCTCAGTCCAGAATCTCGCCCACCCGCCAGAAGTCGTGTTGACAGATTTCCAGACC
CTGGATGGAAGCCAGTACAACCCGGTCAAACAGCAGCTAGTGCGTTACGCCACCAGCTGT
TACAGCTGTTGTCCGCGACTGGCCTCGGTGCTGCTATACTCCGATTATGGGATAGGAGAA
GTGCCCGTGGAGCCCCTGGATGTCCCCTTACCCTCCACGATCAGGCCAGCTTCCCCCGTG
GCCGGGTCTCCAAAGCAGCCGGTGCGTGGCTACTACCGTGGCGCTGTCGGTGGCACGTTT
GACCGCCTGCACAACGCCCACAAGGTGTTGCTCAGTGTCGCGTGCATCCTGGCCCAGGAG
CAGCTTGTGGTGGGAGTAGCAGACAAAGATCTGTTGAAGAGCAAGTTGCTCCCTGAGCTG
CTCCAACCTTATACAGAACGTGTGGAACATCTGAGTGAATTCCTGGTGGACATCAAGCCC
TCCTTGACTTTTGATGTCATCCCCCTGCTGGACCCCTATGGGCCCGCTGGCTCTGACCCC
TCCCTGGAGTTCCTGGTGGTCAGCGAGGAGACCTATCGTGGGGGGATGGCCATCAACCGC
TTCCGCCTTGAGAATGACCTGGAGGAACTTGCTTTGTACCAGATCCAGCTGCTGAAGGAC
CTCAGACATACGGAGAATGAAGAGGACAAAGTCAGCTCCTCCAGCTTCCGCCAGCGAATG
TTGGGGAACCTGCTTCGGCCTCCATATGAAAGGCCAGAGCTCCCCACATGTCTCTATGTA
ATTGGGCTGACTGGCATCAGTGGCTCTGGGAAGAGCTCAATAGCTCAGCGACTGAAGGGC
CTGGGGGCGTTTGTCATTGACAGTGACCACCTGGGTCATCGGGCCTATGCCCCAGGTGGC
CCTGCCTACCAGCCTGTGGTGGAGGCCTTTGGAACAGATATTCTCCATAAAGATGGCATC
ATCAACAGGAAGGTCCTAGGCAGCCGGGTGTTTGGGAATAAGAAGCAGCTGAAGATACTC
ACGGACATTATGTGGCCAATTATCGCAAAGCTGGCCCGAGAGGAGATGGATCGGGCTGTG
GCTGAGGGAAAGCGTGTGTGTGTGATTGATGCCGCTGTGTTGCTTGAAGCCGGCTGGCAG
AACCTGGTCCATGAGGTGTGGACTGCTGTCATCCCAGAGACTGAGGCTGTAAGACGCATT
GTGGAGAGGGATGGCCTCAGTGAAGCCGCGGCTCAAAGCCGGCTGCAGAGCCAGATGAGC
GGGCAGCAGCTTGTGGAACAGAGCCACGTGGTGCTCAGCACCTTGTGGGAGCCGCATATC
ACCCAACGCCAGGTGGAGAAAGCCTGGGCCCTCTTGCAGAAGCGCATTCCCAAGACTCAT
CAGGCCCTCGACTGA
Enzyme 8 GenBank Gene ID AF453478 Link Image
Enzyme 8 GeneCard ID COASY Link Image
Enzyme 8 GenAtlas ID COASY Link Image
Enzyme 8 HGNC ID HGNC:29932 Link Image
Enzyme 8 Chromosome Location 17
Enzyme 8 Locus 17q12-q21
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Daugherty M, Polanuyer B, Farrell M, Scholle M, Lykidis A, de Crecy-Lagard V, Osterman A: Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomics. J Biol Chem. 2002 Jun 14;277(24):21431-9. Epub 2002 Mar 28. [PubMed Link Image]
  2. Aghajanian S, Worrall DM: Identification and characterization of the gene encoding the human phosphopantetheine adenylyltransferase and dephospho-CoA kinase bifunctional enzyme (CoA synthase). Biochem J. 2002 Jul 1;365(Pt 1):13-8. [PubMed Link Image]
  3. Montagna M, Serova O, Sylla BS, Feunteun J, Lenoir GM: A 100-kb physical and transcriptional map around the EDH17B2 gene: identification of three novel genes and a pseudogene of a human homologue of the rat PRL-1 tyrosine phosphatase. Hum Genet. 1995 Nov;96(5):532-8. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 8658
Enzyme 9 Name Phosphopantothenoylcysteine decarboxylase
Enzyme 9 Synonyms
  1. PPC-DC
  2. CoaC
Enzyme 9 Gene Name PPCDC
Enzyme 9 Protein Sequence >Phosphopantothenoylcysteine decarboxylase 
MEPKASCPAAAPLMERKFHVLVGVTGSVAALKLPLLVSKLLDIPGLEVAVVTTERAKHFY
SPQDIPVTLYSDADEWEMWKSRSDPVLHIDLRRWADLLLVAPLDANTLGKVASGICDNLL
TCVMRAWDRSKPLLFCPAMNTAMWEHPITAQQVDQLKAFGYVEIPCVAKKLVCGDEGLGA
MAEVGTIVDKVKEVLFQHSGFQQS
Enzyme 9 Number of Residues 204
Enzyme 9 Molecular Weight 22413
Enzyme 9 Theoretical pI 6.01
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Coenzyme transport and metabolism
Enzyme 9 Specific Function Necessary for the biosynthesis of coenzyme A. Catalyzes the decarboxylation of 4-phosphopantothenoylcysteine to form 4'- phosphopantotheine
Enzyme 9 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
Enzyme 9 Reactions
  • N-[(R)-4'-phosphopantothenoyl]-L-cysteine = pantotheine 4'-phosphate + CO2
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-30
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 10197638 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q96CD2 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name COAC_HUMAN Link Image
Enzyme 9 PDB ID 1QZU Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >384 bp 
ATGTGGAAGAGCCGCTCTGACCCAGTTCTGCACATTGACCTGCGGAGGTGGGCAGACCTC
CTGCTGGTGGCTCCTCTTGATGCCAACACTCTGGGGAAGGTGGCCAGTGGCATCTGTGAC
AACTTGCTTACCTGCGTCATGCGGGCCTGGGACCGCAGCAAGCCCCTGCTCTTCTGCCCG
GCCATGAACACCGCCATGTGGGAGCACCCGATCACAGCGCAGCAGGTAGACCAGCTCAAG
GCCTTTGGCTATGTCGAGATCCCCTGTGTGGCCAAGAAGCTGGTGTGCGGAGATGAAGGT
CTCGGGGCCATGGCTGAAGTGGGGACCATCGTGGACAAAGTGAAAGAAGTCCTCTTCCAG
CACAGTGGCTTCCAGCAGAGTTGA
Enzyme 9 GenBank Gene ID AF182419 Link Image
Enzyme 9 GeneCard ID PPCDC Link Image
Enzyme 9 GenAtlas ID PPCDC Link Image
Enzyme 9 HGNC ID HGNC:28107 Link Image
Enzyme 9 Chromosome Location 15
Enzyme 9 Locus 15q24.2
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. Daugherty M, Polanuyer B, Farrell M, Scholle M, Lykidis A, de Crecy-Lagard V, Osterman A: Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomics. J Biol Chem. 2002 Jun 14;277(24):21431-9. Epub 2002 Mar 28. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 12887
Enzyme 10 Name Probable 10-formyltetrahydrofolate dehydrogenase ALDH1L2
Enzyme 10 Synonyms
  1. Aldehyde dehydrogenase family 1 member L2
Enzyme 10 Gene Name ALDH1L2
Enzyme 10 Protein Sequence >Probable 10-formyltetrahydrofolate dehydrogenase ALDH1L2 
MLRRGSQALRRFSTGRVYFKNKLKLALIGQSLFGQEVYSHLRKEGHRVVGVFTVPDKDGK
ADPLALAAEKDGTPVFKLPKWRVKGKTIKEVAEAYRSVGAELNVLPFCTQFIPMDIIDSP
KHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPND
TVDALYNRFLFPEGIKAMVEAVQLIADGKAPRIPQPEEGATYEGIQKKENAEISWDQSAE
VLHNWIRGHDKVPGAWTEINGQMVTFYGSTLLNSSVPPGEPLEIKGAKKPGLVTKNGLVL
FGNDGKALTVRNLQFEDGKMIPASQYFSTGETSVVELTAEEVKVAETIKVIWAGILSNVP
IIEDSTDFFKSGASSMDVARLVEEIRQKCGGLQLQNEDVYMATKFEGFIQKVVRKLRGED
QEVELVVDYISKEVNEIMVKMPYQCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLA
DVDKAVAAAKDAFENGEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLAL
KTHIGMSVQTFRYFAGWCDKIQGSTIPINQARPNRNLTFTKKEPLGVCAIIIPWNYPLMM
LAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSE
HPDIRKLGFTGSTPIGKQIMKSCAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAV
FFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLL
QYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQNGD
IDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSG
FGKDLGEEALNEYLKTKTVTLEY
Enzyme 10 Number of Residues 923
Enzyme 10 Molecular Weight 101746
Enzyme 10 Theoretical pI Not Available
Enzyme 10 GO Classification Not Available
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions
  • 10-formyltetrahydrofolate + NADP+ + H2O = tetrahydrofolate + CO2 + NADPH
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 74355155 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q3SY69 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name AL1L2_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 BC103934 Link Image
Enzyme 10 GeneCard ID Q3SY69 Link Image
Enzyme 10 GenAtlas ID ALDH1L2 Link Image
Enzyme 10 HGNC ID HGNC:26777 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References Not Available
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 16513
Enzyme 11 Name Pantothenate kinase 2 (Hallervorden-Spatz syndrome) (HCG39342, isoform CRA_c)
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name PANK2
Enzyme 11 Protein Sequence >Pantothenate kinase 2 (Hallervorden-Spatz syndrome) (HCG39342, isoform CRA_c) 
MPAFIQMGRDKNFSSLHTVFCATGGGAYKFEQDFLTIGDLQLCKLDELDCLIKGILYIDS
VGFNGRSQCYYFENPADSEKCQKLPFDLKNPYPLLLVNIGSGVSILAVYSKDNYKRVTGT
SLGGGTFFGLCCLLTGCTTFEEALEMASRGDSTKVDKLVRDIYGGDYERFGLPGWAVASS
FGNMMSKEKREAVSKEDLARATLITITNNIGSIARMCALNENINQVVFVGNFLRINTIAM
RLLAYALDYWSKGQLKALFSEHEGYFGAVGALLELLKIP
Enzyme 11 Number of Residues 279
Enzyme 11 Molecular Weight 30754
Enzyme 11 Theoretical pI 5.88
Enzyme 11 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • pantothenate kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • coenzyme A biosynthesis
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • physiological process
Component
—
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
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 B1AK33 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name B1AK33_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 AL353194 Link Image
Enzyme 11 GeneCard ID B1AK33 Link Image
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location 20
Enzyme 11 Locus 20p13
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 16975
Enzyme 12 Name FASN variant protein
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name FASN variant protein
Enzyme 12 Protein Sequence >FASN variant protein 
RQRPRPPSPPRSSLPLRRAPASLSAARTAARALTRAAMEEVVIAGMSGKLPESENLQEFW
DNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRFDASFFGVHPKQAHTMDPQLRLLL
EVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEALSRDPETLVGYSMVGCQRAMMANR
LSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRL
GMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLARRVYATILNAGTNTDGFKEQGVTF
PSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQELNGITRALCATRQEPLLIG
STKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPALLDGRLQVVDQPLPV
RGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATLPRLLRASGRTPEAVQKLLEQGLR
HSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGPEVQQVPAGERPLWFICSGMGTQW
RGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLSTDESTFDDIVHSFVSLTAIQIGL
IDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAVLAAYWRGQCIKEAHLPPGAMAAV
GLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFEFVEQLRKEGVFAKEVRTGGMAFH
SYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEAQWHSSLARTSSAEYNVNNLVSPV
LFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCTIIPLMKKDHRDNLEFFLAGIGRL
HLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSLAWDVPAAEDFPNGSGSPSAAIYN
IDTSSESPDHYLVDHTLDGRVLFPATGYLSIVWKTLARALGLGVEQLPVVFEDVVLHQAT
ILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQWDDPDPRLFDHPESPTPNPTEPL
FLAQAEVYKELRLRGYDYGPHFQGILEASLEGDSGRLLWKDNWVSFMDTMLQMSILGSAK
HGLYLPTRVTAIHIDPATHRQKLYTLQDKAQVADVVVSRWLRVTVAGGVHISGLHTESAP
RRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQLCKGLVQALQTKVTQQGLKMVVPG
LDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQVLAQERPKLPEDPLLSGLLDSPA
LKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLLSPHPLLQLSYTATDRHPQALEAA
QAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVAALGDPASALSNMVAALREGGFLL
LHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESLFSRVSLRLVGLKKSFYGSTLFLC
RRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRPVWLKAINCATSGVVGLVNCLRRE
PGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGDLVMNVYRDGAWGAFRHFLLEEDK
PEEPTAHAFVSTLTRGDLSSIRWVCSSLRHAQPTCPGAQLCTVYYASLNFRDIMLATGKL
SPDAIPGKWTSQDSLLGMEFSGRDASGKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLE
EAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAE
KRAYLQARFPQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATH
GRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFNESSADWREVWALVQAGIRDGVV
RPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQVLAEEPEAVLKGAKPKLMSAISKTFCPA
HKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVST
SNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLD
RVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPGLAVQWGAI
GDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLNQPHMVLSSFVLAEKAAAYRDRDS
QRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREVRQLT
LRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLRSLLVNPEGPTLMRLNSVQSSERP
LFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLDSIHSLAAYYIDCIRQVQPEGPYR
VAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPGCEAEA
ETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAAVDLIIKSHQGLDRQELSFAARSF
YYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGADYNLSQVCDGKVSVHVIEGDHRT
LLEGSGLESIISIIHSSLAEPRVSVREG
Enzyme 12 Number of Residues 2548
Enzyme 12 Molecular Weight 277373
Enzyme 12 Theoretical pI 6.63
Enzyme 12 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • oxidoreductase activity
  • phosphopantetheine binding
  • transferase activity
  • vitamin binding
Process
  • biosynthesis
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid biosynthesis
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
—
Enzyme 12 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
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 Q4LE83 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name Q4LE83_HUMAN Link Image
Enzyme 12 PDB ID 1XKT Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence Not Available
Enzyme 12 GenBank Gene ID AB209988 Link Image
Enzyme 12 GeneCard ID Q4LE83 Link Image
Enzyme 12 GenAtlas ID FASN variant protein Link Image
Enzyme 12 HGNC ID HGNC:3594 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
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 16976
Enzyme 13 Name Acyl carrier protein
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name Not Available
Enzyme 13 Protein Sequence >Acyl carrier protein 
RVLSAYVSRLPAAFAPLPRVRMLAVARPLSTALCSAGTQTRLGTLQPALVLAQVPGRVTQ
LCRQYSDMPPLTLEGIQDRVLYVLKLYDKIDPEKLSVNSHFMKDLGLDSLDQVEIIMAME
DEFG
Enzyme 13 Number of Residues 124
Enzyme 13 Molecular Weight 13715
Enzyme 13 Theoretical pI 7.26
Enzyme 13 GO Classification
Function
  • binding
  • cofactor binding
  • phosphopantetheine binding
  • vitamin binding
Process
—
Component
—
Enzyme 13 General Function Lipid transport and metabolism
Enzyme 13 Specific Function Carrier of the growing fatty acid chain in fatty acid biosynthesis
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 A4UCS3 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name A4UCS3_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 EF036490 Link Image
Enzyme 13 GeneCard ID A4UCS3 Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs Not Available
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available