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Database: UniProt
Entry: O29108
LinkDB: O29108
Original site: O29108 
ID   PUR2_ARCFU              Reviewed;         470 AA.
AC   O29108;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JAN-2019, entry version 119.
DE   RecName: Full=Phosphoribosylamine--glycine ligase;
DE            EC=6.3.4.13;
DE   AltName: Full=GARS;
DE   AltName: Full=Glycinamide ribonucleotide synthetase;
DE   AltName: Full=Phosphoribosylglycinamide synthetase;
GN   Name=purD; OrderedLocusNames=AF_1157;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM
OS   9628 / NBRC 100126).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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   -!- 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.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000305}.
DR   EMBL; AE000782; AAB90089.1; -; Genomic_DNA.
DR   PIR; D69394; D69394.
DR   RefSeq; WP_010878654.1; NC_000917.1.
DR   ProteinModelPortal; O29108; -.
DR   SMR; O29108; -.
DR   STRING; 224325.AF1157; -.
DR   EnsemblBacteria; AAB90089; AAB90089; AF_1157.
DR   GeneID; 24794765; -.
DR   KEGG; afu:AF_1157; -.
DR   eggNOG; arCOG04415; Archaea.
DR   eggNOG; COG0151; LUCA.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   OrthoDB; 58022at2157; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000002199; 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; 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.
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    470       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_0000151508.
FT   DOMAIN      115    354       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     142    203       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   METAL       324    324       Magnesium or manganese.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       326    326       Magnesium or manganese.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
SQ   SEQUENCE   470 AA;  51750 MW;  C3B90CED22DCD353 CRC64;
     MKVLVVDAGG RGNAIAHAFS RSEQVKEIYI APGNGGSEFF EKCKIAELDG KKIPSIRAID
     EIVRFAKKCE VDLAYIGPEE PLSLGLVDRL EEEGIPAVGP KKEATILEAS KCWAKDFLKR
     IGVPIPEYAN FDNPEEAKEY IREKFNNGIV VKADGLAAGK GVYVCDSVEE ALRAVDEIMV
     QKKFGEAGNR IVVEERLRGI EVAFTAMTDG KTVKPFGHAR DYKRAFDSDD IEGLRDFYIG
     LTKKFYTKAQ IEQLYREGKL INPNTGGMGA VSPHPAVTEE VEQRIMEMVV EPIIENFDKE
     FKGVLYPVIM LVEENGELIP KVLEINVRDC DPGAEAKLPR LKSDMAEISM AVVEGRLDEV
     EMRFSSDYCV AVCAVSGALK GREGLKPGYP ADHYTSQPIT GIEEAMKEAI IYANGIAKTN
     GYVTTGGRVL TVVGMGQSIE EARSKAYSAL EKISFPGMRY RRTIGLDVPE
//
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