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Database: UniProt
Entry: M1WWW2_PSEP2
LinkDB: M1WWW2_PSEP2
Original site: M1WWW2_PSEP2 
ID   M1WWW2_PSEP2            Unreviewed;       425 AA.
AC   M1WWW2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   05-JUN-2019, entry version 43.
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   ECO:0000313|EMBL:CCH49353.1};
GN   OrderedLocusNames=BN4_12118 {ECO:0000313|EMBL:CCH49353.1};
OS   Pseudodesulfovibrio piezophilus (strain DSM 21447 / JCM 15486 /
OS   C1TLV30) (Desulfovibrio piezophilus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae.
OX   NCBI_TaxID=1322246 {ECO:0000313|EMBL:CCH49353.1, ECO:0000313|Proteomes:UP000011724};
RN   [1] {ECO:0000313|EMBL:CCH49353.1, ECO:0000313|Proteomes:UP000011724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX   PubMed=23383081; DOI=10.1371/journal.pone.0055130;
RA   Pradel N., Ji B., Gimenez G., Talla E., Lenoble P., Garel M.,
RA   Tamburini C., Fourquet P., Lebrun R., Bertin P., Denis Y.,
RA   Pophillat M., Barbe V., Ollivier B., Dolla A.;
RT   "The first genomic and proteomic characterization of a deep-sea
RT   sulfate reducer: insights into the piezophilic lifestyle of
RT   Desulfovibrio piezophilus.";
RL   PLoS ONE 8:e55130-e55130(2013).
RN   [2] {ECO:0000313|Proteomes:UP000011724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX   PubMed=23961312; DOI=10.4056/sigs.3777412;
RA   Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M.,
RA   Amann R., Schreiber L.;
RT   "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT   deltaproteobacterium specialized in disproportionating inorganic
RT   sulfur compounds.";
RL   Stand. Genomic Sci. 8:58-68(2013).
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}.
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DR   EMBL; FO203427; CCH49353.1; -; Genomic_DNA.
DR   RefSeq; WP_015415397.1; NC_020409.1.
DR   STRING; 1322246.BN4_12118; -.
DR   EnsemblBacteria; CCH49353; CCH49353; BN4_12118.
DR   KEGG; dpi:BN4_12118; -.
DR   PATRIC; fig|879567.3.peg.2258; -.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   OrthoDB; 932854at2; -.
DR   BioCyc; DPIE1322246:BN4_RS10660-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000011724; Chromosome.
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:UP000011724};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:CCH49353.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011724}.
FT   DOMAIN      107    313       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   425 AA;  45075 MW;  C29225A1C463015E CRC64;
     MKILVVGGGG REHALCWKLS LNPKVERILC APGNGGTAQI GENFPIKDDD IPALVALARD
     EEVDLVVVGP ELPLVLGLEN ALRQEGIPCF GPSAYAANLE GSKAFSKNVM HDAGVPTAAF
     RVFDEYDAAV AFIKKQGAPI VVKADGLAAG KGVIVATTEE EALEAVENMM VKKAFGSAGD
     RVVIEETLAG EEASFLAFCD GLHYALLPSS QDHKAVFEGD TGPNTGGMGA YSPAPILPKE
     KYEETAELCI KPILRHLASK GEPFKGVLYA GLIYTADGPS VLEYNVRFGD PECQPLLMRL
     ETDLLEIMFA CIDGKLDQVD VTSTAQTACG VVMAAEGYPG DYPKGMPVTG LDAADAMEGV
     KVFQAGTVFA DGEILTAGGR VLCVTALGDG LADAQKRAYE AVEKVHFDKS YYRRDIADKG
     LKRLK
//
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