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Database: UniProt
Entry: A5UMK4
LinkDB: A5UMK4
Original site: A5UMK4 
ID   PUR2_METS3              Reviewed;         436 AA.
AC   A5UMK4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   01-OCT-2014, entry version 48.
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=Msm_1227;
OS   Methanobrevibacter smithii (strain PS / ATCC 35061 / DSM 861).
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PS / ATCC 35061 / DSM 861;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M.,
RA   Henrissat B., Fulton R., Latreille P., Kim K., Wilson R.K.,
RA   Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to
RT   the human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
CC   -!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP
CC       + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide.
CC       {ECO:0000255|HAMAP-Rule:MF_00138}.
CC   -!- COFACTOR: 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}.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP-
CC       Rule:MF_00138}.
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DR   EMBL; CP000678; ABQ87432.1; -; Genomic_DNA.
DR   RefSeq; YP_001273800.1; NC_009515.1.
DR   ProteinModelPortal; A5UMK4; -.
DR   STRING; 420247.Msm_1227; -.
DR   EnsemblBacteria; ABQ87432; ABQ87432; Msm_1227.
DR   GeneID; 5216011; -.
DR   KEGG; msi:Msm_1227; -.
DR   eggNOG; COG0151; -.
DR   HOGENOM; HOG000033464; -.
DR   KO; K01945; -.
DR   OMA; YKGFLYA; -.
DR   BioCyc; MSMI420247:GHWZ-1263-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 1.
DR   Gene3D; 3.40.50.20; -; 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; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR016185; PreATP-grasp_dom.
DR   InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR   InterPro; IPR000115; PRibGlycinamide_synth.
DR   InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
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   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    436       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_1000018828.
FT   DOMAIN      106    318       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00138}.
FT   NP_BIND     133    196       ATP. {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       276    276       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       288    288       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       288    288       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       290    290       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
SQ   SEQUENCE   436 AA;  47267 MW;  FE37BFFD1F9487F9 CRC64;
     MKVLVVGTGA REHAIADALK DDVELYCYMS KVNPGISKIA EFAQGDEGEI EKVAKFAVDN
     NIDIAFIGPE APLGKGIVDE LEKNGISCVG PSQSAARIET DKSFMRKLFE DYDIEGSLVY
     KVFDNYDDVS AFLDDFDRDV VVKPVGLTGG KGVKIVGDHL KDNQEAKEYS KEVIDNAMGG
     FTQVIIEERL IGEEFTIQAF CDGTHLAPMP AAQDHPHAFE GDVGAITGGM GSYSDKGGLL
     PFLSQDDYDE AVKIMEATLK AIAKEAEPYK GILYGQFMLT ADGPKLIEYN ARFGDPEAMN
     VLPLLKTPLA DVCQAIVDGN LDKVEFNDKA SVCKYIVPDG YPETSHAGET IEVDEKTIED
     LGAKVFYAAV GLEDDEIHLS GSRALGIVAS GDSIEEAEKI AEKACACIKG NVYHRSDVGT
     TDLVNKRVEH MKEILN
//
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