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Database: UniProt
Entry: Q9ZF44
LinkDB: Q9ZF44
Original site: Q9ZF44 
ID   PUR2_LACLA              Reviewed;         412 AA.
AC   Q9ZF44;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   05-DEC-2018, entry version 118.
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=LL1513;
GN   ORFNames=L153005;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus
OS   lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CHCC373;
RX   PubMed=9797284;
RA   Nilsson D., Kilstrup M.;
RT   "Cloning and expression of the Lactococcus lactis purDEK genes,
RT   required for growth in milk.";
RL   Appl. Environ. Microbiol. 64:4321-4327(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.GR-1697R;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K.,
RA   Weissenbach J., Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK05611.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AJ000883; CAA04374.1; -; Genomic_DNA.
DR   EMBL; AE005176; AAK05611.1; ALT_INIT; Genomic_DNA.
DR   PIR; A86814; A86814.
DR   RefSeq; NP_267669.1; NC_002662.1.
DR   ProteinModelPortal; Q9ZF44; -.
DR   SMR; Q9ZF44; -.
DR   STRING; 272623.L153005; -.
DR   PaxDb; Q9ZF44; -.
DR   EnsemblBacteria; AAK05611; AAK05611; L153005.
DR   GeneID; 1115170; -.
DR   KEGG; lla:L153005; -.
DR   PATRIC; fig|272623.7.peg.1623; -.
DR   eggNOG; ENOG4105C12; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   HOGENOM; HOG000033463; -.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000002196; 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    412       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_0000151455.
FT   DOMAIN      108    309       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00138}.
FT   NP_BIND     134    190       ATP. {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       279    279       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       281    281       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   CONFLICT     46     46       D -> H (in Ref. 1; CAA04374).
FT                                {ECO:0000305}.
FT   CONFLICT    215    215       G -> E (in Ref. 1; CAA04374).
FT                                {ECO:0000305}.
SQ   SEQUENCE   412 AA;  44289 MW;  EAAD0D69997E1C02 CRC64;
     MKILVIGSGG REHALAKKFM ESPQVEEVFV APGNSGMEKD GIQIVDISEL SNDKLVKFAQ
     NQNIGLTFVG PETALMNGVV DAFIKAELPI FGPNKMAAEL EGSKDFAKSI MKKYGVPTAD
     YATFDSLEPA LAYLDEKGVP LVIKADGLAA GKGVTVAFDI ETAKSALADI FSGSQGKVVI
     EEFLDGEEFS LFSFIHDGKI YPMPIAQDHK RAFDGDKGPN TGGMGAYSPV LHISKEVVNE
     ALEKVVKPTV AGMIEEGKSF TGVLYAGLIL TEDGVKTIEF NARFGDPETQ VVLPRLKSDL
     AQAIIDILAG NEPTLEWLES GVTLGVVVAA EGYPSQAKLG LILPEIPEGL NVYYAGVSKN
     ENNQLISSGG RVYLVSETGE DVKSTQKLLY EKLDKLENDG FFYRHDIGSR AI
//
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