(data stored in SCRATCH9089 zone)

SWISSPROT: PUR2_PASMU

ID   PUR2_PASMU              Reviewed;         429 AA.
AC   P57829;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   11-DEC-2019, entry version 118.
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}; OrderedLocusNames=PM0224;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-
CC         (5-phospho-D-ribosyl)glycinamide + phosphate; Xref=Rhea:RHEA:17453,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:58089, ChEBI:CHEBI:58457,
CC         ChEBI:CHEBI:456216; EC=6.3.4.13; Evidence={ECO:0000255|HAMAP-
CC         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; N(1)-
CC       (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC       diphosphate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00138}.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000255|HAMAP-
CC       Rule:MF_00138}.
DR   EMBL; AE004439; AAK02308.1; -; Genomic_DNA.
DR   RefSeq; WP_005723617.1; NC_002663.1.
DR   SMR; P57829; -.
DR   PRIDE; P57829; -.
DR   EnsemblBacteria; AAK02308; AAK02308; PM0224.
DR   KEGG; pmu:PM0224; -.
DR   PATRIC; fig|272843.6.peg.232; -.
DR   eggNOG; ENOG4105C12; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   HOGENOM; HOG000033463; -.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   BioCyc; PMUL272843:G1FZ8-235-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000000809; 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;
DR   PRODOM; P57829.
DR   SWISS-2DPAGE; P57829.
KW   ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..429
FT                   /note="Phosphoribosylamine--glycine ligase"
FT                   /id="PRO_0000151468"
FT   DOMAIN          109..316
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT   NP_BIND         135..196
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT   METAL           286
FT                   /note="Magnesium or manganese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT   METAL           288
FT                   /note="Magnesium or manganese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
SQ   SEQUENCE   429 AA;  45872 MW;  65080956ED18F865 CRC64;
     MNILIIGNGG REHALAWKVA QSPMAEKVFV APGNAGTALE EKVENVAISA TDVEKLVAFA
     QANHIGLTIV GPEAPLVIGV VDAFRAAGLK IFGPTKAAAQ LEGSKAFTKD FLARHHIPTA
     EYQNFTEVEP ALAYLREKGA PIVVKADGLA AGKGVIVAMT LDEAEAAVKE MLSGNAFGEA
     GSRVVIEEFL DGEEASFIVM VDGKNVEPMA TSQDHKRVGE NDTGLNTGGM GAYSPAPVVT
     PEIHERIMQQ VIYPTVNGMA AEGNIYTGFL YAGLMIMPNG QPKVIEFNCR FGDPETQPIM
     LRLESDLVEL CLAACDGKLD QKKSQWCEQA SLGIVLAAEG YPGDYRKGDE ITGIESAVEN
     QKVFLAGVEN KDGKLVTNGG RVVCVTALGD TVYDAQQQAL ALAEQVKWTG RFYRRDIGYR
     AVAREKNNA
//

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