PUR2_LACLA
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 03-AUG-2022, entry version 129.
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 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; DOI=10.1128/aem.64.11.4321-4327.1998;
RA Nilsson D., Kilstrup M.;
RT "Cloning and expression of the Lactococcus lactis purDEK genes, required
RT 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., Weissenbach J.,
RA 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-beta-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate;
CC Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681,
CC ChEBI:CHEBI:143788, 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; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC 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};
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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 RefSeq; WP_014570649.1; NC_002662.1.
DR AlphaFoldDB; Q9ZF44; -.
DR SMR; Q9ZF44; -.
DR STRING; 272623.L153005; -.
DR PaxDb; Q9ZF44; -.
DR EnsemblBacteria; AAK05611; AAK05611; L153005.
DR KEGG; lla:L153005; -.
DR PATRIC; fig|272623.7.peg.1623; -.
DR eggNOG; COG0151; Bacteria.
DR HOGENOM; CLU_027420_3_1_9; -.
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 PANTHER; PTHR43472; PTHR43472; 1.
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; Reference proteome.
FT CHAIN 1..412
FT /note="Phosphoribosylamine--glycine ligase"
FT /id="PRO_0000151455"
FT DOMAIN 108..309
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT BINDING 134..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00138"
FT CONFLICT 46
FT /note="D -> H (in Ref. 1; CAA04374)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="G -> E (in Ref. 1; CAA04374)"
FT /evidence="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
