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Database: UniProt
Entry: V8C657_9HELI
LinkDB: V8C657_9HELI
Original site: V8C657_9HELI 
ID   V8C657_9HELI            Unreviewed;       453 AA.
AC   V8C657;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   05-JUN-2019, entry version 31.
DE   RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|HAMAP-Rule:MF_00138};
DE            EC=6.3.4.13 {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=GARS {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
GN   Name=purD {ECO:0000256|HAMAP-Rule:MF_00138};
GN   ORFNames=HMPREF2086_01653 {ECO:0000313|EMBL:ETD22854.1};
OS   Helicobacter macacae MIT 99-5501.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1357400 {ECO:0000313|EMBL:ETD22854.1, ECO:0000313|Proteomes:UP000018731};
RN   [1] {ECO:0000313|EMBL:ETD22854.1, ECO:0000313|Proteomes:UP000018731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 99-5501 {ECO:0000313|EMBL:ETD22854.1,
RC   ECO:0000313|Proteomes:UP000018731};
RX   PubMed=25212613;
RA   Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA   Fox J.G.;
RT   "Draft genome sequences of six enterohepatic helicobacter species
RT   isolated from humans and one from rhesus macaques.";
RL   Genome Announc. 2:e00857-14(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC         N(1)-(5-phospho-D-ribosyl)glycinamide + phosphate;
CC         Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58089,
CC         ChEBI:CHEBI:58457, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00138};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC       ribose 1-diphosphate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00138}.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000256|HAMAP-
CC       Rule:MF_00138}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ETD22854.1}.
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DR   EMBL; AZJI01000007; ETD22854.1; -; Genomic_DNA.
DR   STRING; 1357400.HMPREF2086_01653; -.
DR   EnsemblBacteria; ETD22854; ETD22854; HMPREF2086_01653.
DR   PATRIC; fig|1357400.3.peg.2223; -.
DR   BioCyc; GCF_000507845-HMP:HMPREF2086_RS08665-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000018731; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.90.600.10; -; 1.
DR   HAMAP; MF_00138; GARS; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR   InterPro; IPR000115; PRibGlycinamide_synth.
DR   InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
DR   InterPro; IPR037123; PRibGlycinamide_synth_C_sf.
DR   InterPro; IPR020559; PRibGlycinamide_synth_CS.
DR   InterPro; IPR020562; PRibGlycinamide_synth_N.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF01071; GARS_A; 1.
DR   Pfam; PF02843; GARS_C; 1.
DR   Pfam; PF02844; GARS_N; 1.
DR   SMART; SM01210; GARS_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR00877; purD; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00184; GARS; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018731};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:ETD22854.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018731}.
FT   DOMAIN      131    341       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION        1     27       Disordered. {ECO:0000256|MobiDB-lite:
FT                                V8C657}.
SQ   SEQUENCE   453 AA;  48894 MW;  6B8D5A9122F626E5 CRC64;
     MSSNPPSTSQ SYSAQSSSTS QNPTNQKSIL IVGNGGREYA LGEHLRSDKR VGEIYFAIGN
     AGTKTLGQNV ELKSNEEITT FCKEKQIDWV IIGGESALVA GLSDELAKEG IKAFGPSKDA
     AKLEGSKAFM KDFLCEFQIP TAKYIQTDNP QEALDFARTL TPPIVVKASG LCAGKGVIIA
     QTYDEAKQSI QSMLSGKSFG EAGLRIVVEE YLVGYELSVF AICDGEDFIT LPACQDHKQL
     YDGDKGPNTG GMGAYTPTPL CDKTLMQKIE SRIFAPTLEG MKKRGTPFCG VLFAGIMVVE
     KGGELEPYLL EFNVRFGDPE CEVLMPLLQT PLLDICEAVK SKNLKNLQVS FSDKHCVAVV
     LASHNYPFGS SIPHTIKITP YDENLGRVHY AGVSESSEDK EHSMLASGGR VALAVGIADS
     LPKAQANAYT IAKSIQFEGA IYRKDIADKA IKP
//
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