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Q5HAM9

- Q5HAM9_EHRRW

UniProt

Q5HAM9 - Q5HAM9_EHRRW

Protein

Phosphoribosylformylglycinamidine synthase subunit PurL

Gene

probable purL

Organism
Ehrlichia ruminantium (strain Welgevonden)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (15 Feb 2005)
      Previous versions | rss
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    Functioni

    Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.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 annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei266 – 2661UniRule annotation
    Binding sitei322 – 3221ATPUniRule annotation
    Metal bindingi324 – 3241Magnesium 1UniRule annotation
    Active sitei326 – 3261Proton acceptorUniRule annotation
    Binding sitei347 – 3471SubstrateUniRule annotation
    Metal bindingi348 – 3481Magnesium 2UniRule annotation
    Binding sitei487 – 4871SubstrateUniRule annotation
    Metal bindingi516 – 5161Magnesium 2UniRule annotation
    Binding sitei747 – 7471ATPUniRule annotation
    Binding sitei784 – 7841ATP; via carbonyl oxygen and amide nitrogenUniRule annotation
    Binding sitei787 – 7871SubstrateUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    LigaseUniRule annotationImported

    Keywords - Biological processi

    Purine biosynthesisUniRule annotation

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciERUM254945:GJ2L-715-MONOMER.
    UniPathwayiUPA00074; UER00128.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoribosylformylglycinamidine synthase subunit PurLUniRule annotation (EC:6.3.5.3UniRule annotation)
    Short name:
    FGAM synthaseUniRule annotation
    Alternative name(s):
    Formylglycinamide ribonucleotide amidotransferase subunit IIUniRule annotation
    Glutamine amidotransferase PurLUniRule annotation
    Phosphoribosylformylglycinamidine synthase subunit IIUniRule annotation
    Gene namesi
    Name:probable purLImported
    Synonyms:purLUniRule annotationImported
    Ordered Locus Names:Erum6510Imported, ERWE_CDS_06830Imported
    OrganismiEhrlichia ruminantium (strain Welgevonden)Imported
    Taxonomic identifieri254945 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia
    ProteomesiUP000001021: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    CytoplasmUniRule annotation

    Interactioni

    Subunit structurei

    Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.UniRule annotation

    Protein-protein interaction databases

    STRINGi254945.Erum6510.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5HAM9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni557 – 5593Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the FGAMS family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0046.
    HOGENOMiHOG000238228.
    KOiK01952.
    OMAiQAVVFKI.
    OrthoDBiEOG6FNHHR.

    Family and domain databases

    Gene3Di3.30.1330.10. 2 hits.
    HAMAPiMF_00420. PurL_2.
    InterProiIPR010918. AIR_synth_C_dom.
    IPR000728. AIR_synth_N_dom.
    IPR010074. PRibForGlyAmidine_synth_II.
    IPR016188. PurM_N-like.
    [Graphical view]
    PfamiPF00586. AIRS. 2 hits.
    PF02769. AIRS_C. 2 hits.
    [Graphical view]
    SUPFAMiSSF55326. SSF55326. 2 hits.
    SSF56042. SSF56042. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q5HAM9-1 [UniParc]FASTAAdd to Basket

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    MIIRIGIADK TLLENYRNTT LTVYTIDTQK NLDQETINKI GTLLTNPITQ     50
    RFFTFIYNNV ELNYQEVNTT NNYNLLNIFN ANWSLEKSFL PGVTDNVGNT 100
    TKCMIKEALK CDFSLDVITS QVIFSQETVP QEKDILKIYN PLIEYCKLSI 150
    RKETGFNVRF FGNKQILDLN KLYDNSRTHN TIFIIPYVRQ EDLVPQCITQ 200
    DTCVTAVNLN IQDEELMELS KYGIHGRGGL NLSLEAMKAI QAYFKKINRN 250
    PNDIELETLA QTWSEHCKHN IFSSPIDDII DGLYKHYIKR ATYEINSEIC 300
    VSTFSDNAGA IIFDDNFIIA DKVETHNSPS ALDPFGGAIT GILGVNRDII 350
    GFGKGAKPIL NAYYFCFSES EKELYRDKMC TVSVLPSETI INGVIKGVNS 400
    GGNCSGIPTG LGSVYFDDRF QSKPLVFVGC TGIIPRIIGN TPSHLKGPAD 450
    GDYIVIAGGR TGRDGIHGAT FSSNALTENN SNSTVVQIGD PITQKKLSDA 500
    IIKEARDLNL YNAITDNGAG GLSSSIGEMG NNGFKVELNK VLLKHKNMLP 550
    WEIWVSESQE RMTLAIPPSK FPIFEKIMKK HDVEISIIGT FNNTKKAVVS 600
    YNDSIIMDID INFLHNGIPK THLKTIPWSN IISSAVDTLH NKPLDTELNE 650
    MMQRMNICSK EFISTQYDHE VQGTSVIKPI QGKGRVDGEA IVIRPILSSE 700
    RGLVKSHGLG SSYGEISTYH MAACAIDTAI RNYIAIGGNF HHLALLDNFC 750
    WCDSTNPKRL WQLKNAAQAC YDYAKIFKTP FISGKDSMFN DFKGYNNKGE 800
    PINISAPPSL LISTVGIIEN IHNAITLDVK NPGDLIYILG VTYDELGRSE 850
    YQKYSGLGNN NVPQVRAKHA KKLYKLYSNA VNTNIISSAI ALNLGGLVIG 900
    LIKSLIGGEL GAKIDLSLVP THNIEDNSIK EKVILFSESQ SRILVTIAPH 950
    NKQKFETIFK DIAHANIGII SDTNTLIINN MHIINLNTLK HSYKKFSNMK 1000
    IQAYANAEYI 1010
    Length:1,010
    Mass (Da):112,383
    Last modified:February 15, 2005 - v1
    Checksum:i5BD1D05F49D027DD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR767821 Genomic DNA. Translation: CAH58383.1.
    CR925678 Genomic DNA. Translation: CAI27177.1.
    RefSeqiWP_011155331.1. NC_006832.1.
    YP_180515.1. NC_005295.2.
    YP_197559.1. NC_006832.1.

    Genome annotation databases

    EnsemblBacteriaiCAH58383; CAH58383; Erum6510.
    CAI27177; CAI27177; ERWE_CDS_06830.
    GeneIDi3232585.
    3261422.
    KEGGieru:Erum6510.
    erw:ERWE_CDS_06830.
    PATRICi20581232. VBIEhrRum92411_0723.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR767821 Genomic DNA. Translation: CAH58383.1 .
    CR925678 Genomic DNA. Translation: CAI27177.1 .
    RefSeqi WP_011155331.1. NC_006832.1.
    YP_180515.1. NC_005295.2.
    YP_197559.1. NC_006832.1.

    3D structure databases

    ProteinModelPortali Q5HAM9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 254945.Erum6510.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAH58383 ; CAH58383 ; Erum6510 .
    CAI27177 ; CAI27177 ; ERWE_CDS_06830 .
    GeneIDi 3232585.
    3261422.
    KEGGi eru:Erum6510.
    erw:ERWE_CDS_06830.
    PATRICi 20581232. VBIEhrRum92411_0723.

    Phylogenomic databases

    eggNOGi COG0046.
    HOGENOMi HOG000238228.
    KOi K01952.
    OMAi QAVVFKI.
    OrthoDBi EOG6FNHHR.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00128 .
    BioCyci ERUM254945:GJ2L-715-MONOMER.

    Family and domain databases

    Gene3Di 3.30.1330.10. 2 hits.
    HAMAPi MF_00420. PurL_2.
    InterProi IPR010918. AIR_synth_C_dom.
    IPR000728. AIR_synth_N_dom.
    IPR010074. PRibForGlyAmidine_synth_II.
    IPR016188. PurM_N-like.
    [Graphical view ]
    Pfami PF00586. AIRS. 2 hits.
    PF02769. AIRS_C. 2 hits.
    [Graphical view ]
    SUPFAMi SSF55326. SSF55326. 2 hits.
    SSF56042. SSF56042. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: WelgevondenImported and Welgevonden [ARC-OVI]Imported.
    2. "Comparative genomic analysis of three strains of Ehrlichia ruminantium reveals an active process of genome size plasticity."
      Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.
      J. Bacteriol. 188:2533-2542(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Welgevonden [CIRAD]Imported.

    Entry informationi

    Entry nameiQ5HAM9_EHRRW
    AccessioniPrimary (citable) accession number: Q5HAM9
    Secondary accession number(s): Q5FD98
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 15, 2005
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 75 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