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Database: UniProt
Entry: Q9JXA3
LinkDB: Q9JXA3
Original site: Q9JXA3 
ID   PUR2_NEIMB              Reviewed;         423 AA.
AC   Q9JXA3;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JAN-2019, entry version 110.
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=NMB2151;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C.,
RA   Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F.,
RA   Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D.,
RA   Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D.,
RA   Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E.,
RA   Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M.,
RA   Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M.,
RA   Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R.,
RA   Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; AE002098; AAF42459.1; -; Genomic_DNA.
DR   PIR; E81000; E81000.
DR   RefSeq; NP_275136.1; NC_003112.2.
DR   RefSeq; WP_002225741.1; NC_003112.2.
DR   ProteinModelPortal; Q9JXA3; -.
DR   SMR; Q9JXA3; -.
DR   STRING; 122586.NMB2151; -.
DR   PaxDb; Q9JXA3; -.
DR   PRIDE; Q9JXA3; -.
DR   EnsemblBacteria; AAF42459; AAF42459; NMB2151.
DR   GeneID; 903221; -.
DR   KEGG; nme:NMB2151; -.
DR   PATRIC; fig|122586.8.peg.2745; -.
DR   eggNOG; ENOG4105C12; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   HOGENOM; HOG000033463; -.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   BioCyc; NMEN122586:G1G1B-2095-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000000425; 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;
KW   Reference proteome.
FT   CHAIN         1    423       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_0000151467.
FT   DOMAIN      107    314       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00138}.
FT   NP_BIND     133    194       ATP. {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       284    284       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       286    286       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
SQ   SEQUENCE   423 AA;  44975 MW;  7203DDCAEC2D38E2 CRC64;
     MKLLVIGNGG REHALAWKLA QSPKVETVFV APGNAGTAIE PKLQNIDLTA HQDLIEFCRK
     ENIVFTVVGP EAPLAAGIVD DFRAAGLKIF GPTQYAAQLE SSKDFAKAFM AKYNIPTAQY
     QTFENADAAH DYVNQKGAPI VIKADGLAAG KGVIVAMTLD EAHAAIDDML LDNKMGNAGA
     RVVIEDFLQG EEASFIVMVD GNNVLPMATS QDHKRLLDGD KGLNTGGMGA YSPAPVVTPV
     VYERAMNEII LPTVAGMKAE GHEFTGFLYA GLMIDQSGAP YTIEFNCRFG DPETQPIMSR
     LNSDLSDLVE AAIDGKLDSV TAEWSPQTAV GVVLAAQNYP ETPKKGDIIS GLDAANQIGK
     VFHAGTTANE KGDVLTNGGR VLCVVGLGDN VAQAKAKAYG ALEKISFDGM QYRKDIADKA
     INR
//
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