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Database: UniProt
Entry: Q9F1S9
LinkDB: Q9F1S9
Original site: Q9F1S9 
ID   PUR2_STRSU              Reviewed;         420 AA.
AC   Q9F1S9;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   05-DEC-2018, entry version 77.
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};
OS   Streptococcus suis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DAT1 / Serotype 2;
RX   PubMed=11133943; DOI=10.1128/JB.183.2.500-511.2001;
RA   Sekizaki T., Otani Y., Osaki M., Takamatsu D., Shimoji Y.;
RT   "Evidence for horizontal transfer of the SsuDAT1I restriction-
RT   modification genes to the Streptococcus suis genome.";
RL   J. Bacteriol. 183:500-511(2001).
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; AB045609; BAB20832.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q9F1S9; -.
DR   SMR; Q9F1S9; -.
DR   eggNOG; ENOG4105C12; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   UniPathway; UPA00074; UER00125.
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; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Purine biosynthesis.
FT   CHAIN         1    420       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_0000151493.
FT   DOMAIN      108    314       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00138}.
FT   NP_BIND     134    195       ATP. {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       284    284       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       286    286       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
SQ   SEQUENCE   420 AA;  45333 MW;  14E9C2D29CDF6B9F CRC64;
     MKLLVVGSGG REHAIAKKLL ESEQVEQVFV APGNDGMTLD GIELINIGIS EHSALINFAK
     ENDIAWTFVG PDDALAAGIV DDFEQAGLKA FGPSRLAAEL EWSKDFAKQI MVKYGIPTAA
     FGTFSNFEEA KAYIEEQGAP IVVKADGLAL GKGVVVAETV EQAVEAAREM LLDNKFGDSG
     ARVVIEEFLA GEEFSLFALV NGDQFYILPT AQDHKRAFDG DQGPNTGGMG AYVHVPHLPQ
     SVVDTAVDTI VKPILEGMIT EGRSYLGVLY AGLILTDQGP KVIEFNARFG DPETQIILPR
     LTSDFAQNID DILHKRPTQL TWLNSGVTLG VVVASNGYPL DYEKGVTLPA KTEGDITTYY
     AGARFAENSR ALLSNGGRVY MLVTTADTVQ DAQEKIYSEL KNQDTTGLFY RTDIGSKAVK
//
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