GenomeNet

Database: UniProt
Entry: PUR2_LEPIN
LinkDB: PUR2_LEPIN
Original site: PUR2_LEPIN 
ID   PUR2_LEPIN              Reviewed;         426 AA.
AC   Q8EZT7;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAY-2019, entry version 104.
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=LA_3764;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai
OS   (strain 56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H.,
RA   Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F.,
RA   Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F.,
RA   Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W.,
RA   Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A.,
RA   Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z.,
RA   Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira
RT   interrogans revealed by whole-genome sequencing.";
RL   Nature 422:888-893(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   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000255|HAMAP-
CC       Rule:MF_00138}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN50962.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; AE010300; AAN50962.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_713944.2; NC_004342.2.
DR   SMR; Q8EZT7; -.
DR   EnsemblBacteria; AAN50962; AAN50962; LA_3764.
DR   GeneID; 1153106; -.
DR   KEGG; lil:LA_3764; -.
DR   PATRIC; fig|189518.3.peg.3737; -.
DR   eggNOG; ENOG4105C12; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   HOGENOM; HOG000033463; -.
DR   InParanoid; Q8EZT7; -.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000001408; 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;
KW   Reference proteome.
FT   CHAIN         1    426       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_0000151459.
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;  46244 MW;  F27E9A51BA9F1DD0 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 GKIKGVQAAV KKGAAVVVVL AAQGYPDFYE KNIPLNLPET
     SGQNVHLFHA GTLKKDGKVF SSGGRILGIV AQGADLKSSV DQAYSFLEKI QAPKTFYRKD
     IGYRAL
//
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