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Database: UniProt
Entry: Q88DK2
LinkDB: Q88DK2
Original site: Q88DK2 
ID   PUR2_PSEPK              Reviewed;         431 AA.
AC   Q88DK2;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   05-DEC-2018, entry version 102.
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=PP_4823;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 /
OS   KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M.,
RA   Hance I., Chris Lee P., Holtzapple E.K., Scanlan D., Tran K.,
RA   Moazzez A., Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D.,
RA   Wedler H., Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S.,
RA   Kiewitz C., Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B.,
RA   Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the
RT   metabolically versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN70392.1; -; Genomic_DNA.
DR   RefSeq; NP_746928.1; NC_002947.4.
DR   RefSeq; WP_010955432.1; NC_002947.4.
DR   ProteinModelPortal; Q88DK2; -.
DR   SMR; Q88DK2; -.
DR   STRING; 160488.PP_4823; -.
DR   PRIDE; Q88DK2; -.
DR   EnsemblBacteria; AAN70392; AAN70392; PP_4823.
DR   GeneID; 1043159; -.
DR   KEGG; ppu:PP_4823; -.
DR   PATRIC; fig|160488.4.peg.5147; -.
DR   eggNOG; ENOG4105C12; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   HOGENOM; HOG000033463; -.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   BioCyc; PPUT160488:G1G01-5160-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000000556; 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    431       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_0000151470.
FT   DOMAIN      108    315       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00138}.
FT   NP_BIND     134    195       ATP. {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       285    285       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       287    287       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
SQ   SEQUENCE   431 AA;  45837 MW;  0F55678D9CB72F51 CRC64;
     MKVLIIGSGG REHALAWKVA QDPRVEKVFV APGNAGTAIE AKCENVAIDV CALEQLADFA
     EKNVDLTIVG PEAPLVIGVV DLFRSRGLDC FGPTKGAAQL EGSKAFTKDF LARHEIPTAD
     YQNFTEIEPA LAYLQEKGAP IVIKADGLAA GKGVIVAMTL EEAEAAVRDM LAGNAFGEAG
     SRVVIEEFLD GEEASFIVMV DGHNVLPMAT SQDHKRVGDQ DTGPNTGGMG AYSPAPVVTA
     DVHQRVMDQV IWPTVRGMAE EGNVYTGFLY AGLMIDKAGN PKVIEFNCRF GDPETQPVML
     RLESSLVLLV EAAFAKALDK VEAQWDPRPS LGVVLAAGGY PGDYAKGDVI NGLDAAAKIE
     GKVFHAGTAL KDGKVTTNGG RVLCATAMGS TVADAQQQAY RLAKEVSWNG SFYRSDIGYR
     AIARERGEHQ Q
//
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