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Database: UniProt
Entry: Q465Q9
LinkDB: Q465Q9
Original site: Q465Q9 
ID   PUR2_METBF              Reviewed;         433 AA.
AC   Q465Q9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   13-FEB-2019, entry version 105.
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=Mbar_A3513;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/JB.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P.,
RA   Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R.,
RA   Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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 2 magnesium or manganese ions per subunit.
CC       {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; CP000099; AAZ72383.1; -; Genomic_DNA.
DR   RefSeq; WP_011308422.1; NC_007355.1.
DR   ProteinModelPortal; Q465Q9; -.
DR   SMR; Q465Q9; -.
DR   STRING; 269797.Mbar_A3513; -.
DR   PRIDE; Q465Q9; -.
DR   EnsemblBacteria; AAZ72383; AAZ72383; Mbar_A3513.
DR   GeneID; 3625401; -.
DR   KEGG; mba:Mbar_A3513; -.
DR   eggNOG; arCOG04415; Archaea.
DR   eggNOG; COG0151; LUCA.
DR   HOGENOM; HOG000033464; -.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   OrthoDB; 58022at2157; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000008156; 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    433       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_1000018821.
FT   DOMAIN      110    317       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00138}.
FT   NP_BIND     137    194       ATP. {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       275    275       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       287    287       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       287    287       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       289    289       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
SQ   SEQUENCE   433 AA;  46905 MW;  FE1CFE41937107CC CRC64;
     MKILLIGGGG REHAIAEGIK KSKHNPSLYA LMAKKNPGIA ALCEDFLLEK ETEVEKVVEY
     AKARNIEMAF VGPEAPLAAG VADALWEAGI PVVGPKKSCA IIEFDKAWAR NFMKKYGIEG
     CPEYEVFTEE KPAHDFIEKL GDVAVKPSGL TGGKGVKVMG DQLPDLKAAK AYTSELLEKG
     SVVIEERFIG EEFTLQAFVD GKSLVFFPAV QDHKRAYEGD LGPNTGGMGS YTDAGEILPF
     MLPEDLEKAK KIMQDTVKAL SEETGIGYQG ILYGQFILTA SGPKVVEFNA RFGDPEAMNV
     ISLLETDFVD IMSAVVKGTL GNLPVSFSKK ATVCKYAVPA GYPENPEKDS EVTVEDIGDA
     SIYYASVYEK EGKVYTTSSR AIAVIGIAET IAAAEKIAQN ALENLHGKLF FRKDIGTAAL
     IQKRIDHMKE LRG
//
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