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Database: UniProt
Entry: Q8Z334
LinkDB: Q8Z334
Original site: Q8Z334 
ID   PUR2_SALTI              Reviewed;         429 AA.
AC   Q8Z334;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 1.
DT   05-DEC-2018, entry version 115.
DE   RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000255|HAMAP-Rule:MF_00138};
DE            EC=6.3.4.13 {ECO:0000255|HAMAP-Rule:MF_00138};
DE   AltName: Full=GARS {ECO:0000255|HAMAP-Rule:MF_00138};
DE   AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_00138};
DE   AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000255|HAMAP-Rule:MF_00138};
GN   Name=purD {ECO:0000255|HAMAP-Rule:MF_00138};
GN   OrderedLocusNames=STY3710, t3456;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P.,
RA   Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J.,
RA   Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K.,
RA   Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C.,
RA   Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K.,
RA   Whitehead S., Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella
RT   enterica serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/JB.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J.,
RA   Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2
RT   and CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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:0000255|HAMAP-Rule:MF_00138};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
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:0000255|HAMAP-Rule:MF_00138}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00138}.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000255|HAMAP-
CC       Rule:MF_00138}.
DR   EMBL; AL513382; CAD09469.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO70972.1; -; Genomic_DNA.
DR   RefSeq; NP_457899.1; NC_003198.1.
DR   RefSeq; WP_000866776.1; NZ_UFRG01000003.1.
DR   ProteinModelPortal; Q8Z334; -.
DR   SMR; Q8Z334; -.
DR   STRING; 220341.STY3710; -.
DR   PRIDE; Q8Z334; -.
DR   EnsemblBacteria; AAO70972; AAO70972; t3456.
DR   EnsemblBacteria; CAD09469; CAD09469; CAD09469.
DR   GeneID; 1249966; -.
DR   KEGG; stt:t3456; -.
DR   KEGG; sty:STY3710; -.
DR   PATRIC; fig|220341.7.peg.3782; -.
DR   eggNOG; ENOG4105C12; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   HOGENOM; HOG000033463; -.
DR   KO; K01945; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Complete proteome; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN         1    429       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_0000151476.
FT   DOMAIN      109    316       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00138}.
FT   NP_BIND     135    196       ATP. {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       286    286       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       288    288       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
SQ   SEQUENCE   429 AA;  45670 MW;  943A77FF1E8702BE CRC64;
     MKVLVIGNGG REHALAWKAA QSPLVDTVFV APGNAGTALE PALQNVAIGV TDIPALLSFA
     QNEKIDLTIV GPEAPLVIGV VDAFRAAGLK IFGPTEGAAQ LEGSKAFTKD FLARHQIPTA
     EYQNFTEIEP ALAYLREKGA PIVIKADGLA AGKGVIVAMT LEEAEAAVHD MLAGNAFGDA
     GHRIVIEEFL DGEEASFIVM VDGEHVLPMA TSQDHKRVGN GDTGPNTGGM GAYSPAPVVT
     DEVHQRTMER IIWPTVKGMA AEGNTYTGFL YAGLMIDKQG NPKVIEFNCR FGDPETQPIM
     LRMKSDLVDL CLAACDGKLD EKTSEWDERA SLGVVIAAGG YPGSYSTGDE IHGLPLEEVA
     DGKVFHAGTK LADDDRVLTS GGRVLCATAL GHTVAEAQKR AYALMTDIRW DGSFSRNDIG
     WRAIEREQN
//
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