GenomeNet

Database: UniProt
Entry: A6US04
LinkDB: A6US04
Original site: A6US04 
ID   PUR2_METVS              Reviewed;         443 AA.
AC   A6US04;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   16-JAN-2019, entry version 70.
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=Mevan_1379;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 /
OS   OCM 148 / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci;
OC   Methanococcales; Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000742; ABR55276.1; -; Genomic_DNA.
DR   RefSeq; WP_012066190.1; NC_009634.1.
DR   ProteinModelPortal; A6US04; -.
DR   SMR; A6US04; -.
DR   STRING; 406327.Mevan_1379; -.
DR   EnsemblBacteria; ABR55276; ABR55276; Mevan_1379.
DR   GeneID; 5324746; -.
DR   KEGG; mvn:Mevan_1379; -.
DR   eggNOG; arCOG04415; Archaea.
DR   eggNOG; COG0151; LUCA.
DR   HOGENOM; HOG000033464; -.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   OrthoDB; 58022at2157; -.
DR   BioCyc; MVAN406327:G1G99-1433-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000001107; 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.
FT   CHAIN         1    443       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_1000018830.
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   443 AA;  48771 MW;  766525AA8170DE24 CRC64;
     MKVLLIGGGA REHAIAMALK KNRSVELYTL MKNKNPGIYG LSKEVSFNNE TDIDKIKEFA
     EKIRPELAII GPEAPLGVGA ADLLTEMGIP TVGPKKLPAQ IETSKEFMRN LFKKYNIKGS
     LKYAAFNEYG ENLEKFIDEM TGLGKDVVVK PAGLTGGKGV KVVGEQLKNN DDAKLYAKEV
     FEKSIGGGKI IVEEKLVGVE FTLHGFVDGE NIVFMPAVQD HPHAYNNDEG PITGGMGSYS
     CSNHKLPFLP DDKLDEAKEI MKETVNAIKA EVGPYNGFLY GQFMLTKDGP KIIEYNARFG
     DPEAMNLLPI LKTDFLDVCF GISNGNLDNI NIEFENKATV CKYVVPNGYP ICPVKNKEIL
     VNSNEIEKAG AILFYASVNE ENGKLVITGS RSAAVTGISE RIEDAEKIAQ DAIINFEGEI
     FFRSDIGTKK LIEKRIERMK ELI
//
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