GenomeNet

Database: UniProt
Entry: Q6M079
LinkDB: Q6M079
Original site: Q6M079 
ID   PUR2_METMP              Reviewed;         444 AA.
AC   Q6M079;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JAN-2019, 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=MMP0392;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci;
OC   Methanococcales; Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/JB.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E.,
RA   Hackett M., Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J.,
RA   Major T.A., Moore B.C., Porat I., Palmeiri A., Rouse G.,
RA   Saenphimmachak C., Soell D., Van Dien S., Wang T., Whitman W.B.,
RA   Xia Q., Zhang Y., Larimer F.W., Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable
RT   hydrogenotrophic methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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; BX950229; CAF29948.1; -; Genomic_DNA.
DR   RefSeq; WP_011170336.1; NC_005791.1.
DR   ProteinModelPortal; Q6M079; -.
DR   SMR; Q6M079; -.
DR   STRING; 267377.MMP0392; -.
DR   EnsemblBacteria; CAF29948; CAF29948; MMP0392.
DR   GeneID; 2762213; -.
DR   KEGG; mmp:MMP0392; -.
DR   PATRIC; fig|267377.15.peg.396; -.
DR   eggNOG; arCOG04415; Archaea.
DR   eggNOG; COG0151; LUCA.
DR   HOGENOM; HOG000033464; -.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   OrthoDB; 58022at2157; -.
DR   BioCyc; MMAR267377:MMP_RS02095-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000000590; 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    444       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_1000018827.
FT   DOMAIN      109    324       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00138}.
FT   NP_BIND     140    202       ATP. {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       282    282       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       294    294       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       294    294       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       296    296       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
SQ   SEQUENCE   444 AA;  48796 MW;  01467220AD6B49BE CRC64;
     MKVLLIGGGA REHAIAMALK KNELVELYTL MKNKNPGIYA LSEEVSFNSE TDVPAIKEFA
     EKIKPEIAVI GPESPLGVGA SDLLEEMGIP TVGPKKLPAQ IETSKEFMRN LFKKYEIDGS
     LKYAAFNDYG TELEGFIDEM TSLGKDVVVK PAGLTGGKGV KVVGEQLKDN EEAKIYAKEV
     FDKSIGGGKI IIEEKLVGVE FTLHGFVDGE NIVFMPAVQD HPHAYNNDEG PITGGMGSYS
     CPNHGLPFLS EEMLDKAEKI MEKTVNSINL EVGPYKGFLY GQFMLTADGP KIIEYNARFG
     DPEAMNLLPI LKTDFLDVCF AIAEGKLDKI NIEFENKATV CKYVVPNGYP IDPVRNKELA
     VDEKAIEDAN AILFYASINE ENGKLYITGS RSAAVVGISE NIEEAEKIAQ KAIENFKGEV
     YYRSDIGTLD LIKKRVERVK KLAK
//
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