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A1KW75

- A1KW75_NEIMF

UniProt

A1KW75 - A1KW75_NEIMF

Protein

Phosphoribosylformylglycinamidine synthase

Gene

purL

Organism
Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (06 Feb 2007)
      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.UniRule annotationSAAS 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 sitei683 – 6831ATP; via carbonyl oxygenUniRule annotation
    Metal bindingi684 – 6841MagnesiumUniRule annotation
    Metal bindingi723 – 7231MagnesiumUniRule annotation
    Metal bindingi727 – 7271MagnesiumUniRule annotation
    Metal bindingi889 – 8891MagnesiumUniRule annotation
    Binding sitei891 – 8911ATPUniRule annotation
    Active sitei1167 – 11671NucleophileUniRule annotation
    Active sitei1290 – 12901UniRule annotation
    Active sitei1292 – 12921UniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi316 – 32712ATPUniRule 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

    BioCyciNMEN272831:GJDX-1866-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 annotationImported
    Ordered Locus Names:NMC1972Imported
    OrganismiNeisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)Imported
    Taxonomic identifieri272831 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
    ProteomesiUP000002286: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotationSAAS annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    CytoplasmUniRule annotationSAAS annotation

    Interactioni

    Subunit structurei

    Monomer.UniRule annotationSAAS annotation

    Protein-protein interaction databases

    STRINGi272831.NMC1972.

    Structurei

    3D structure databases

    ProteinModelPortaliA1KW75.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    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.
    OMAiGEGHAEF.
    OrthoDBiEOG6FNHHR.

    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.
    IPR022940. PRibForGlyAmidine_synth_bac.
    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.

    A1KW75-1 [UniParc]FASTAAdd to Basket

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    MRAESMSVVL PLRGVTALSD FRVEKLLQKA AALGLPEVKL SSEFWYFAGS     50
    EKALDAATVE KLQALLAAQS VEQTPKAREG LHLFLVTPRL GTISPWASKA 100
    TNIAENCGLA GIERIERGMA VWLEGALTDE QKQQWAALLH DRMTESVLPD 150
    FQTASKLFHH LESETFSTVD VLGGGKEALV KANTEMGLAL SADEIDYLVE 200
    NYQALQRNPS DVELMMFAQA NSEHCRHKIF NADFILNGEK QPKSLFGMIR 250
    DTHNAHPEGT VVAYKDNSSV IEGAKIERFY PNAAENQGYR FHEEDTHIIM 300
    KVETHNHPTA IAPFAGAATG AGGEIRDEGA TGKGSRPKAG LTGFTVSNLN 350
    IPGLKQPWEQ DYGKPEHISS PLDIMIEGPI GGAAFNNEFG RPNLLGYFRT 400
    FEEKFDGQVR GYHKPIMIAG GLGSIQAQQT HKDEIPEGAL LIQLGGPGML 450
    IGLGGGAASS MDTGTNDASL DFNSVQRGNP EIERRAQEVI DRCWQLGDKN 500
    PIISIHDVGA GGLSNAFPEL VNDAGRGAVF ELREVPLEEH GLTPLQIWCN 550
    ESQERYVLSI LEKDLDTFRA ICERERCPFA VVGTATDDGH LKVRDDLFAN 600
    NPIDLPLNVL LGKPPKTTRT DKTVTPSKKP FHADDIDITE AAYRVLHLPA 650
    VAAKNFLITI GDRSVGGMTH RDQMVGKYQT PVADCAVTMM GFNTYRGEAM 700
    SMGEKPTVAL FDAPASGRMC VGEAITNIAA VNIGDIGNIK LSANWMAACG 750
    NEGEDEKLYR TVEAVSKACQ ALDLSIPVGK DSLSMKTVWQ DGEEKKSVVS 800
    PLSLIISAFA PVQDVRKTVT PELKNVEDSV LLFVDLGFGK ARMGGSAFGQ 850
    VYNNMSGDAP DLDDTGRLKA FYNVIQQLVA EDKLLAYHDR SDGGLFAVLV 900
    EMAFAGRCGL DIDLNLLLAQ TFITNHTALS QSLRTEEVKA LAEWQETIAR 950
    TLFNEELGAV IQVRKQDVAD IINLFYQQQL HHNVFEIGTL TDENTLIIRD 1000
    GQTHLISDNL IKLQQTWQET SHQIQRLRDN PACADSEFAL IGDNDRSALF 1050
    ANLKFDVNED IAAPFINSGA KPKIAILREQ GVNGQIEMAA AFTRAGFDAY 1100
    DVHMSDLMAG RFRLADFKML AACGGFSYGD VLGAGEGWAK SILFHPALRD 1150
    QFAAFFADPD TLTLGVCNGC QMVSNLAEII PGAEAWPKFK RNLSEQFEAR 1200
    LSMVHVPKSA SLILNEMQGS SLPVVVSHGE GRADFALHGG NISADLGIAL 1250
    QYVDGQNQVT QTYPLNPNGS PQGIAGVTNA DGRVTIMMPH PERVYRAAQM 1300
    SWKPEDWTEL SGWYRLFAGA RKALG 1325
    Length:1,325
    Mass (Da):144,502
    Last modified:February 6, 2007 - v1
    Checksum:iC2C446817EF39BDA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM421808 Genomic DNA. Translation: CAM11131.1.
    RefSeqiWP_011799023.1. NC_008767.1.
    YP_975899.1. NC_008767.1.

    Genome annotation databases

    EnsemblBacteriaiCAM11131; CAM11131; NMC1972.
    GeneIDi4676582.
    KEGGinmc:NMC1972.
    PATRICi20354458. VBINeiMen17609_2457.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM421808 Genomic DNA. Translation: CAM11131.1 .
    RefSeqi WP_011799023.1. NC_008767.1.
    YP_975899.1. NC_008767.1.

    3D structure databases

    ProteinModelPortali A1KW75.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272831.NMC1972.

    Protein family/group databases

    MEROPSi C56.972.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAM11131 ; CAM11131 ; NMC1972 .
    GeneIDi 4676582.
    KEGGi nmc:NMC1972.
    PATRICi 20354458. VBINeiMen17609_2457.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00128 .
    BioCyci NMEN272831:GJDX-1866-MONOMER.

    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.
    IPR022940. PRibForGlyAmidine_synth_bac.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700532 / DSM 15464 / FAM18Imported.

    Entry informationi

    Entry nameiA1KW75_NEIMF
    AccessioniPrimary (citable) accession number: A1KW75
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 6, 2007
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 70 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 proteomeImported

    External Data

    Dasty 3