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O15067

- PUR4_HUMAN

UniProt

O15067 - PUR4_HUMAN

Protein

Phosphoribosylformylglycinamidine synthase

Gene

PFAS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 4 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate By similarity.By similarity

    Catalytic activityi

    ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei706 – 7061ATP; via carbonyl oxygenBy similarity
    Metal bindingi707 – 7071MagnesiumBy similarity
    Metal bindingi746 – 7461MagnesiumBy similarity
    Metal bindingi750 – 7501MagnesiumBy similarity
    Metal bindingi909 – 9091MagnesiumBy similarity
    Binding sitei911 – 9111ATPBy similarity
    Active sitei1158 – 11581NucleophileBy similarity
    Active sitei1297 – 12971By similarity
    Active sitei1299 – 12991By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi322 – 33312ATPSequence AnalysisAdd
    BLAST
    Nucleotide bindingi402 – 4043ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphoribosylformylglycinamidine synthase activity Source: UniProtKB

    GO - Biological processi

    1. 'de novo' IMP biosynthetic process Source: UniProtKB
    2. glutamine metabolic process Source: UniProtKB-KW
    3. nucleobase-containing small molecule metabolic process Source: Reactome
    4. purine nucleobase metabolic process Source: Reactome
    5. purine ribonucleoside monophosphate biosynthetic process Source: Reactome
    6. response to drug Source: Ensembl
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Purine biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS11329-MONOMER.
    ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
    UniPathwayiUPA00074; UER00128.

    Protein family/group databases

    MEROPSiC56.972.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoribosylformylglycinamidine synthase (EC:6.3.5.3)
    Short name:
    FGAM synthase
    Short name:
    FGAMS
    Alternative name(s):
    Formylglycinamide ribonucleotide amidotransferase
    Short name:
    FGAR amidotransferase
    Short name:
    FGAR-AT
    Formylglycinamide ribotide amidotransferase
    Gene namesi
    Name:PFAS
    Synonyms:KIAA0361
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:8863. PFAS.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13381338Phosphoribosylformylglycinamidine synthasePRO_0000100401Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei569 – 5691Phosphoserine3 Publications
    Modified residuei619 – 6191Phosphothreonine2 Publications
    Modified residuei623 – 6231Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO15067.
    PaxDbiO15067.
    PRIDEiO15067.

    PTM databases

    PhosphoSiteiO15067.

    Expressioni

    Gene expression databases

    ArrayExpressiO15067.
    BgeeiO15067.
    CleanExiHS_PFAS.
    GenevestigatoriO15067.

    Organism-specific databases

    HPAiHPA022140.
    HPA022886.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EPB41P111711EBI-1052653,EBI-1050906
    HLA-BP304801EBI-1052653,EBI-1054175
    MCCP235081EBI-1052653,EBI-307531
    TFE3P195321EBI-1052653,EBI-1048957
    TNFRSF10DQ9UBN61EBI-1052653,EBI-1044859
    TRAF6Q9Y4K31EBI-1052653,EBI-359276
    VHLP403371EBI-1052653,EBI-301246

    Protein-protein interaction databases

    BioGridi111221. 50 interactions.
    IntActiO15067. 5 interactions.
    STRINGi9606.ENSP00000313490.

    Structurei

    3D structure databases

    ProteinModelPortaliO15067.
    SMRiO15067. Positions 304-572, 1063-1302.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1064 – 1302239Glutamine amidotransferase type-1Add
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the FGAMS family.Curated

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiCOG0046.
    HOGENOMiHOG000261358.
    HOVERGENiHBG108309.
    InParanoidiO15067.
    KOiK01952.
    OMAiPEPLNGP.
    OrthoDBiEOG7353X4.
    PhylomeDBiO15067.
    TreeFamiTF106371.

    Family and domain databases

    Gene3Di3.30.1330.10. 2 hits.
    3.40.50.880. 1 hit.
    HAMAPiMF_00419. PurL_1.
    InterProiIPR010918. AIR_synth_C_dom.
    IPR000728. AIR_synth_N_dom.
    IPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR010073. PRibForGlyAmidine_synth.
    IPR016188. PurM_N-like.
    [Graphical view]
    PfamiPF00586. AIRS. 1 hit.
    PF02769. AIRS_C. 2 hits.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    SSF55326. SSF55326. 2 hits.
    SSF56042. SSF56042. 2 hits.
    TIGRFAMsiTIGR01735. FGAM_synt. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O15067-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPVLHFYVR PSGHEGAAPG HTRRKLQGKL PELQGVETEL CYNVNWTAEA     50
    LPSAEETKKL MWLFGCPLLL DDVARESWLL PGSNDLLLEV GPRLNFSTPT 100
    STNIVSVCRA TGLGPVDRVE TTRRYRLSFA HPPSAEVEAI ALATLHDRMT 150
    EQHFPHPIQS FSPESMPEPL NGPINILGEG RLALEKANQE LGLALDSWDL 200
    DFYTKRFQEL QRNPSTVEAF DLAQSNSEHS RHWFFKGQLH VDGQKLVHSL 250
    FESIMSTQES SNPNNVLKFC DNSSAIQGKE VRFLRPEDPT RPSRFQQQQG 300
    LRHVVFTAET HNFPTGVCPF SGATTGTGGR IRDVQCTGRG AHVVAGTAGY 350
    CFGNLHIPGY NLPWEDPSFQ YPGNFARPLE VAIEASNGAS DYGNKFGEPV 400
    LAGFARSLGL QLPDGQRREW IKPIMFSGGI GSMEADHISK EAPEPGMEVV 450
    KVGGPVYRIG VGGGAASSVQ VQGDNTSDLD FGAVQRGDPE MEQKMNRVIR 500
    ACVEAPKGNP ICSLHDQGAG GNGNVLKELS DPAGAIIYTS RFQLGDPTLN 550
    ALEIWGAEYQ ESNALLLRSP NRDFLTHVSA RERCPACFVG TITGDRRIVL 600
    VDDRECPVRR NGQGDAPPTP LPTPVDLELE WVLGKMPRKE FFLQRKPPML 650
    QPLALPPGLS VHQALERVLR LPAVASKRYL TNKVDRSVGG LVAQQQCVGP 700
    LQTPLADVAV VALSHEELIG AATALGEQPV KSLLDPKVAA RLAVAEALTN 750
    LVFALVTDLR DVKCSGNWMW AAKLPGEGAA LADACEAMVA VMAALGVAVD 800
    GGKDSLSMAA RVGTETVRAP GSLVISAYAV CPDITATVTP DLKHPEGRGH 850
    LLYVALSPGQ HRLGGTALAQ CFSQLGEHPP DLDLPENLVR AFSITQGLLK 900
    DRLLCSGHDV SDGGLVTCLL EMAFAGNCGL QVDVPVPRVD VLSVLFAEEP 950
    GLVLEVQEPD LAQVLKRYRD AGLHCLELGH TGEAGPHAMV RVSVNGAVVL 1000
    EEPVGELRAL WEETSFQLDR LQAEPRCVAE EERGLRERMG PSYCLPPTFP 1050
    KASVPREPGG PSPRVAILRE EGSNGDREMA DAFHLAGFEV WDVTMQDLCS 1100
    GAIGLDTFRG VAFVGGFSYA DVLGSAKGWA AAVTFHPRAG AELRRFRKRP 1150
    DTFSLGVCNG CQLLALLGWV GGDPNEDAAE MGPDSQPARP GLLLRHNLSG 1200
    RYESRWASVR VGPGPALMLR GMEGAVLPVW SAHGEGYVAF SSPELQAQIE 1250
    ARGLAPLHWA DDDGNPTEQY PLNPNGSPGG VAGICSCDGR HLAVMPHPER 1300
    AVRPWQWAWR PPPFDTLTTS PWLQLFINAR NWTLEGSC 1338
    Length:1,338
    Mass (Da):144,734
    Last modified:January 11, 2011 - v4
    Checksum:i273405025B701DAF
    GO

    Sequence cautioni

    The sequence BAA20816.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1326 – 13261F → S(PubMed:10548741)Curated
    Sequence conflicti1326 – 13261F → S in BAA20816. (PubMed:9205841)Curated
    Sequence conflicti1326 – 13261F → S in AAI46769. (PubMed:15489334)Curated
    Sequence conflicti1326 – 13261F → S in AAI67158. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191P → S.3 Publications
    Corresponds to variant rs9891699 [ dbSNP | Ensembl ].
    VAR_055008
    Natural varianti367 – 3671P → L.3 Publications
    Corresponds to variant rs4791641 [ dbSNP | Ensembl ].
    VAR_055009
    Natural varianti481 – 4811F → Y.
    Corresponds to variant rs35217368 [ dbSNP | Ensembl ].
    VAR_055010
    Natural varianti621 – 6211L → P.7 Publications
    Corresponds to variant rs11078738 [ dbSNP | Ensembl ].
    VAR_055011

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB002359 mRNA. Translation: BAA20816.1. Different initiation.
    AC135178 Genomic DNA. No translation available.
    BC146768 mRNA. Translation: AAI46769.1.
    BC167158 mRNA. Translation: AAI67158.1.
    CCDSiCCDS11136.1.
    RefSeqiNP_036525.1. NM_012393.2.
    UniGeneiHs.573976.

    Genome annotation databases

    EnsembliENST00000314666; ENSP00000313490; ENSG00000178921.
    GeneIDi5198.
    KEGGihsa:5198.
    UCSCiuc002gkr.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB002359 mRNA. Translation: BAA20816.1 . Different initiation.
    AC135178 Genomic DNA. No translation available.
    BC146768 mRNA. Translation: AAI46769.1 .
    BC167158 mRNA. Translation: AAI67158.1 .
    CCDSi CCDS11136.1.
    RefSeqi NP_036525.1. NM_012393.2.
    UniGenei Hs.573976.

    3D structure databases

    ProteinModelPortali O15067.
    SMRi O15067. Positions 304-572, 1063-1302.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111221. 50 interactions.
    IntActi O15067. 5 interactions.
    STRINGi 9606.ENSP00000313490.

    Chemistry

    DrugBanki DB00142. L-Glutamic Acid.
    DB00130. L-Glutamine.

    Protein family/group databases

    MEROPSi C56.972.

    PTM databases

    PhosphoSitei O15067.

    Proteomic databases

    MaxQBi O15067.
    PaxDbi O15067.
    PRIDEi O15067.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000314666 ; ENSP00000313490 ; ENSG00000178921 .
    GeneIDi 5198.
    KEGGi hsa:5198.
    UCSCi uc002gkr.3. human.

    Organism-specific databases

    CTDi 5198.
    GeneCardsi GC17P008152.
    H-InvDB HIX0019361.
    HGNCi HGNC:8863. PFAS.
    HPAi HPA022140.
    HPA022886.
    MIMi 602133. gene.
    neXtProti NX_O15067.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0046.
    HOGENOMi HOG000261358.
    HOVERGENi HBG108309.
    InParanoidi O15067.
    KOi K01952.
    OMAi PEPLNGP.
    OrthoDBi EOG7353X4.
    PhylomeDBi O15067.
    TreeFami TF106371.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00128 .
    BioCyci MetaCyc:HS11329-MONOMER.
    Reactomei REACT_1776. Purine ribonucleoside monophosphate biosynthesis.

    Miscellaneous databases

    ChiTaRSi PFAS. human.
    GenomeRNAii 5198.
    NextBioi 20106.
    PROi O15067.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15067.
    Bgeei O15067.
    CleanExi HS_PFAS.
    Genevestigatori O15067.

    Family and domain databases

    Gene3Di 3.30.1330.10. 2 hits.
    3.40.50.880. 1 hit.
    HAMAPi MF_00419. PurL_1.
    InterProi IPR010918. AIR_synth_C_dom.
    IPR000728. AIR_synth_N_dom.
    IPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR010073. PRibForGlyAmidine_synth.
    IPR016188. PurM_N-like.
    [Graphical view ]
    Pfami PF00586. AIRS. 1 hit.
    PF02769. AIRS_C. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52317. SSF52317. 1 hit.
    SSF55326. SSF55326. 2 hits.
    SSF56042. SSF56042. 2 hits.
    TIGRFAMsi TIGR01735. FGAM_synt. 1 hit.
    PROSITEi PS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human phosphoribosylformylglycinamide amidotransferase (FGARAT): regional mapping, complete coding sequence, isolation of a functional genomic clone, and DNA sequence analysis."
      Patterson D., Bleskan J., Gardiner K., Bowersox J.
      Gene 239:381-391(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-19; LEU-367 AND PRO-621.
    2. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS SER-19; LEU-367 AND PRO-621.
      Tissue: Brain.
    3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS SER-19; LEU-367 AND PRO-621.
    5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-619 AND THR-623, VARIANT [LARGE SCALE ANALYSIS] PRO-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569 AND THR-619, VARIANT [LARGE SCALE ANALYSIS] PRO-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, VARIANT [LARGE SCALE ANALYSIS] PRO-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPUR4_HUMAN
    AccessioniPrimary (citable) accession number: O15067
    Secondary accession number(s): A6H8V8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 140 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3