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Database: UniProt
Entry: Q9KF52
LinkDB: Q9KF52
Original site: Q9KF52 
ID   PUR2_BACHD              Reviewed;         428 AA.
AC   Q9KF52;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JAN-2019, entry version 117.
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}; OrderedLocusNames=BH0634;
OS   Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM
OS   9153 / C-125).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N.,
RA   Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S.,
RA   Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus
RT   halodurans and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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 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. {ECO:0000255|HAMAP-Rule:MF_00138}.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000255|HAMAP-
CC       Rule:MF_00138}.
DR   EMBL; BA000004; BAB04353.1; -; Genomic_DNA.
DR   PIR; B83729; B83729.
DR   RefSeq; WP_010896810.1; NC_002570.2.
DR   ProteinModelPortal; Q9KF52; -.
DR   SMR; Q9KF52; -.
DR   STRING; 272558.BH0634; -.
DR   PRIDE; Q9KF52; -.
DR   EnsemblBacteria; BAB04353; BAB04353; BAB04353.
DR   KEGG; bha:BH0634; -.
DR   eggNOG; ENOG4105C12; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   OrthoDB; 932854at2; -.
DR   BioCyc; BHAL272558:G1G3A-706-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000001258; 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    428       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_0000151435.
FT   DOMAIN      107    313       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00138}.
FT   NP_BIND     133    194       ATP. {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       283    283       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       285    285       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
SQ   SEQUENCE   428 AA;  46304 MW;  85B59E32FAC8D168 CRC64;
     MNVLVIGSGG REHTIAWKFA QSEKVERVYV APGNDGMSDV ATCVAISEQD HDQLVAFAKE
     NKIGLTFVGP EVPLLAGIVD RFQEEGLRVF GPSKRAAEIE GSKSYAKQVM KTYNIPTGSY
     EVFTSFDEAK AYVEAEGVPI VIKADGLAAG KGVVVALTNE EAIAALDDML NQDKFGGAGA
     RVVIEEYLEG EELSLMAFVH GETVIPMVGA QDHKRAFDGD QGPNTGGMGA YSPVPQFSDV
     QLKQAVNEIL IPTARALMQE ERSFTGILYA GLMMTADGPK VIEFNARFGD PETQVVLPRL
     KSDLVNVIES LLDGQEPELE WDEQAVLGVV LATKGYPGSY EKGYTISGLE QLEDDTLVFH
     AGTKREEEEL VTNGGRVLLV AKQASTLREA QAAVYEELNK VKSDGLFYRK DIGSKAIAER
     AVSSQTEQ
//
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