Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A1WNW9

- A1WNW9_VEREI

UniProt

A1WNW9 - A1WNW9_VEREI

Protein

Phosphoribosylformylglycinamidine synthase

Gene

purL

Organism
Verminephrobacter eiseniae (strain EF01-2)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (06 Feb 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.UniRule annotation

    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.UniRule annotationSAAS annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei684 – 6841ATP; via carbonyl oxygenUniRule annotation
    Metal bindingi685 – 6851MagnesiumUniRule annotation
    Metal bindingi724 – 7241MagnesiumUniRule annotation
    Metal bindingi728 – 7281MagnesiumUniRule annotation
    Metal bindingi895 – 8951MagnesiumUniRule annotation
    Binding sitei897 – 8971ATPUniRule annotation
    Active sitei1177 – 11771NucleophileUniRule annotation
    Active sitei1298 – 12981UniRule annotation
    Active sitei1300 – 13001UniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi317 – 32812ATPUniRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
    2. glutamine metabolic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    LigaseUniRule annotationSAAS annotationImported

    Keywords - Biological processi

    Purine biosynthesisUniRule annotationSAAS annotation

    Keywords - Ligandi

    ATP-bindingUniRule annotationSAAS annotation, MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciVEIS391735:GHY5-3653-MONOMER.
    UniPathwayiUPA00074; UER00128.

    Protein family/group databases

    MEROPSiC56.972.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoribosylformylglycinamidine synthaseUniRule annotation (EC:6.3.5.3UniRule annotation)
    Short name:
    FGAM synthaseUniRule annotation
    Short name:
    FGAMSUniRule annotation
    Alternative name(s):
    Formylglycinamide ribonucleotide amidotransferaseUniRule annotation
    Gene namesi
    Name:purLUniRule annotation
    Ordered Locus Names:Veis_3609Imported
    OrganismiVerminephrobacter eiseniae (strain EF01-2)Imported
    Taxonomic identifieri391735 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeVerminephrobacter
    ProteomesiUP000000374: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    CytoplasmUniRule annotation

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi391735.Veis_3609.

    Structurei

    3D structure databases

    ProteinModelPortaliA1WNW9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1084 – 1316233Glutamine amidotransferase type-1UniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 glutamine amidotransferase type-1 domain.UniRule annotation
    Contains glutamine amidotransferase type-1 domain.SAAS annotation
    In the N-terminal section; belongs to the FGAMS family.UniRule annotation

    Keywords - Domaini

    Glutamine amidotransferaseUniRule annotationSAAS annotation

    Phylogenomic databases

    eggNOGiCOG0046.
    HOGENOMiHOG000261359.
    KOiK01952.
    OMAiMSPREIW.
    OrthoDBiEOG6FNHHR.

    Family and domain databases

    Gene3Di3.30.1330.10. 2 hits.
    3.40.50.880. 1 hit.
    3.90.650.10. 1 hit.
    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. 3 hits.
    TIGRFAMsiTIGR01735. FGAM_synt. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A1WNW9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTLAGGNAL SPFRARQLQS ALADIHPGIT GIAARFVHLV LTDTAPAPAQ     50
    QQRLAALLRY GDPYAGPVDG CAIIVTPRLG TLSPWASKAT DIARNCGLAV 100
    RHLERSTEYR IRLRAGRLTD AERDRIAALL HDRMTESVLF DPAGLAALFT 150
    ALPPARMEHV DVLGAGLAAL AAANTRLGLA LADQEMEYLV SAFTGLARNP 200
    TEVELMMFAQ ANSEHCRHKI FNARFAIDGV AQEPSLFDMI RHTHQRAPGH 250
    TLVAYSDNAA VMQGHLVEQF AAKMTDGADP SCAHTYAYSY QKSSSTEHLL 300
    MKVETHNHPT AISPWPGAAT GAGGEIRDEG ATGRGARPRA GLTGFSVSRL 350
    WGSQIGRPGH IASALQIMLE GPLGAAAFNN EFGRPNLAGY FREYEQRVGC 400
    GADAVVRGYH KPIMLAGGLG VIDAALVRKI AFPAGTLLVQ LGGPGMRIGM 450
    GGGAASSMAT GSNAAGLDFD SVQRGNPEIQ RRAQEVINHC AAQGAANPIL 500
    AIHDVGAGGL SNALPELIHD AGRGARLDLR AVPLEDSGMS AMEIWSNESQ 550
    ERYVLAIAPE SLAQLRSFCE RERCPLAVLG SATEERQLVL HDSAATAADQ 600
    QLPVNLPMGV LLGQPPRMQR NASSLRRRFV PLDLSGLPLH KAVTDVLAHP 650
    TVASKRFLVS IGDRTVGGLV HRDQMVGPWQ VPVADCAITL ADYQGFAGAA 700
    MAIGERTPLA ALDAPASGRM AVAEAITNLL AAPIELARVK LSANWMAACG 750
    EPGEDAALYA TVEAVGLELC PALGLAIPVG KDSLSMRTQW REGAGQTTVS 800
    SPVSLIVSAF AALTDVRGSL TPQLDATEAE TTLVLIDLGR GRNRMGASIL 850
    GQTLEQSGCP EKDGVPDLDA PQDLLALVDA VNALRAQGRL LAYHDRSDGG 900
    LLATVAEMAF AGQVGVALNV DLLVTEGDGI GDSRMDTGDA KNWAGQVHAR 950
    REERTLEALF SEELGVVLQV RTAERNEVMQ TLRAHGLARW SHFIGSTRPA 1000
    GPRVLQVWRD AQPVFSAPLA DLQRAWDTVS WKICRQRDNP DSADAEHAAA 1050
    GDPTDPGLHL HLQPTFDAPE PPAAPGLRLA RPRVAILREQ GVNSHVEMAY 1100
    AFTEAGFAAC DVHMTDLQTG RVRLADFKGL VACGGFSYGD TLGAGIGWAR 1150
    SISFNPALAA QFQGFFARGD TFGLGVCNGC QMFAELADII PGAQYWPRFT 1200
    TNQSQRFESR LSLVQVTESP SLFLQGMAGS RLPVPVAHGE GYADFRQRGD 1250
    AAQAIAALRF VDNHGAVTER YPFNPNGSPG GLTGVTTADG RFTALMPHPE 1300
    RVFRNIQMSW TPGERSALSP WMRLWRNARR WVG 1333
    Length:1,333
    Mass (Da):142,090
    Last modified:February 6, 2007 - v1
    Checksum:iB763C28198478E9C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000542 Genomic DNA. Translation: ABM59326.1.
    RefSeqiYP_998344.1. NC_008786.1.

    Genome annotation databases

    EnsemblBacteriaiABM59326; ABM59326; Veis_3609.
    GeneIDi4692772.
    KEGGivei:Veis_3609.
    PATRICi24021031. VBIVerEis120356_3893.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000542 Genomic DNA. Translation: ABM59326.1 .
    RefSeqi YP_998344.1. NC_008786.1.

    3D structure databases

    ProteinModelPortali A1WNW9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 391735.Veis_3609.

    Protein family/group databases

    MEROPSi C56.972.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABM59326 ; ABM59326 ; Veis_3609 .
    GeneIDi 4692772.
    KEGGi vei:Veis_3609.
    PATRICi 24021031. VBIVerEis120356_3893.

    Phylogenomic databases

    eggNOGi COG0046.
    HOGENOMi HOG000261359.
    KOi K01952.
    OMAi MSPREIW.
    OrthoDBi EOG6FNHHR.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00128 .
    BioCyci VEIS391735:GHY5-3653-MONOMER.

    Family and domain databases

    Gene3Di 3.30.1330.10. 2 hits.
    3.40.50.880. 1 hit.
    3.90.650.10. 1 hit.
    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. 3 hits.
    TIGRFAMsi TIGR01735. FGAM_synt. 1 hit.
    PROSITEi PS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.
      , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
      Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: EF01-2Imported.

    Entry informationi

    Entry nameiA1WNW9_VEREI
    AccessioniPrimary (citable) accession number: A1WNW9
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 6, 2007
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 64 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Miscellaneous

    In Gram-negative bacteria and most eukaryotes, FGAM synthase is only formed by PurL, a single polypeptide of 140 kDa (large PurL). However in Gram-positive bacteria and archaebacteria, phosphoribosylformylglycinamidine synthase is composed of three separate proteins: PurL (small PurL), PurQ and PurS.UniRule annotation

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3