PUR7_LACLA
ID PUR7_LACLA Reviewed; 236 AA.
AC O68830;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase;
DE EC=6.3.2.6;
DE AltName: Full=SAICAR synthetase;
GN Name=purC; OrderedLocusNames=LL1533; ORFNames=L177350;
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115.
RC STRAIN=CHCC285;
RX PubMed=9683487; DOI=10.1128/jb.180.15.3900-3906.1998;
RA Kilstrup M., Jessing S.G., Wichmand-Jorgensen S.B., Madsen M., Nilsson D.;
RT "Activation control of pur gene expression in Lactococcus lactis: proposal
RT for a consensus activator binding sequence based on deletion analysis and
RT site-directed mutagenesis of purC and purD promoter regions.";
RL J. Bacteriol. 180:3900-3906(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP +
CC L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-
CC 4-carboxamido]succinate + ADP + 2 H(+) + phosphate;
CC Xref=Rhea:RHEA:22628, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58443,
CC ChEBI:CHEBI:77657, ChEBI:CHEBI:456216; EC=6.3.2.6;
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC -!- SIMILARITY: Belongs to the SAICAR synthetase family. {ECO:0000305}.
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DR EMBL; AE005176; AAK05631.1; -; Genomic_DNA.
DR EMBL; AF054888; AAC32329.1; -; Genomic_DNA.
DR PIR; E86816; E86816.
DR RefSeq; NP_267689.1; NC_002662.1.
DR RefSeq; WP_010906022.1; NC_002662.1.
DR AlphaFoldDB; O68830; -.
DR SMR; O68830; -.
DR STRING; 272623.L177350; -.
DR PaxDb; O68830; -.
DR EnsemblBacteria; AAK05631; AAK05631; L177350.
DR KEGG; lla:L177350; -.
DR PATRIC; fig|272623.7.peg.1644; -.
DR eggNOG; COG0152; Bacteria.
DR HOGENOM; CLU_061495_2_0_9; -.
DR OMA; EFCYKND; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR CDD; cd01415; SAICAR_synt_PurC; 1.
DR HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR033934; SAICAR_synt_PurC.
DR InterPro; IPR001636; SAICAR_synth.
DR InterPro; IPR018236; SAICAR_synthetase_CS.
DR Pfam; PF01259; SAICAR_synt; 1.
DR TIGRFAMs; TIGR00081; purC; 1.
DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..236
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_0000100833"
SQ SEQUENCE 236 AA; 27136 MW; BD8E02C8E27F0076 CRC64;
MEKEKLLYEG KAKKLYFTDD SEVLWVEYCD QATALNGARK EQITGKGALN NQITSLIFEK
LNAEGLETHF IEKLSKTEQL NRKVSIIPLE VVLRNVVAGS FAKRFGLEEG IVLQEPIVEF
YYKDDALDDP FINDEHVRFL NIATYSEIEF LKSETRKINE ILKKIWAEIG LTLVDFKLEF
GRLADGRIIL ADEISPDTSR LWDANGQHMD KDVFRRNIGD LVETYTEVLN LLENAK