GenomeNet

Database: UniProt
Entry: Q72V31
LinkDB: Q72V31
Original site: Q72V31 
ID   PUR2_LEPIC              Reviewed;         426 AA.
AC   Q72V31;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   05-DEC-2018, entry version 95.
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=LIC_10472;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar
OS   copenhageni (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=267671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130;
RX   PubMed=15028702; DOI=10.1128/JB.186.7.2164-2172.2004;
RA   Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA   Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A.,
RA   Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H.,
RA   Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H.,
RA   Ferro E.S., Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A.,
RA   Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R.,
RA   Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T.,
RA   Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R.,
RA   de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA   Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA   Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals
RT   novel insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
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   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000255|HAMAP-
CC       Rule:MF_00138}.
DR   EMBL; AE016823; AAS69093.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q72V31; -.
DR   SMR; Q72V31; -.
DR   STRING; 267671.LIC10472; -.
DR   PaxDb; Q72V31; -.
DR   EnsemblBacteria; AAS69093; AAS69093; LIC_10472.
DR   KEGG; lic:LIC_10472; -.
DR   eggNOG; ENOG4105C12; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000007037; Chromosome I.
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    426       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_0000151458.
FT   DOMAIN      113    320       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00138}.
FT   NP_BIND     139    200       ATP. {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       290    290       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       292    292       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
SQ   SEQUENCE   426 AA;  46258 MW;  D0F4ABC2A9349E68 CRC64;
     MQVKLKVLLI GSGGRESAIA FYLRKSVLLS ELKVFPGNGG FPDQELLPPD SFQVLDKNSV
     QSFLKQNPFD LIVVGPEDPL VAGFADWAAE LNIPVFGPDS FCAQVEGSKD FAKSLMTEAK
     IPTAEYKTFS EYSDSLKYLE SKSIPIVIKA DGLAAGKGVT VATSKEMAQT ALKEIFKDKK
     FGSSGNQVVI EEFMEGQEAS IFAISDGDSY FLLPAAQDHK RAFDGDQGPN TGGMGAYCPA
     PVISESILQK VKEQIFDPMF DLFRKKGHPY RGLLYAGLMI SPNGEPKVVE FNCRFGDPET
     QCVLAMLDGD LLELLYRAST GKIKGIQAAV KKGAAVVVVL AAQGYPDFYE KNIPLNLPET
     SGQNVHLFHA GTLKKDGKVF SSGGRILGIV AQGADLKSSV DQAYSFLEKI QAPKTFYRKD
     IGYRAL
//
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