PUR7_LYSSC
ID PUR7_LYSSC Reviewed; 236 AA.
AC B1HTV1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase {ECO:0000255|HAMAP-Rule:MF_00137};
DE EC=6.3.2.6 {ECO:0000255|HAMAP-Rule:MF_00137};
DE AltName: Full=SAICAR synthetase {ECO:0000255|HAMAP-Rule:MF_00137};
GN Name=purC {ECO:0000255|HAMAP-Rule:MF_00137}; OrderedLocusNames=Bsph_0211;
OS Lysinibacillus sphaericus (strain C3-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=444177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3-41;
RX PubMed=18296527; DOI=10.1128/jb.01652-07;
RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA Berry C., Yuan Z.;
RT "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT sphaericus C3-41 and comparison with those of closely related Bacillus
RT species.";
RL J. Bacteriol. 190:2892-2902(2008).
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00137};
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 {ECO:0000255|HAMAP-Rule:MF_00137}.
CC -!- SIMILARITY: Belongs to the SAICAR synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00137}.
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DR EMBL; CP000817; ACA37842.1; -; Genomic_DNA.
DR RefSeq; WP_012292011.1; NC_010382.1.
DR AlphaFoldDB; B1HTV1; -.
DR SMR; B1HTV1; -.
DR EnsemblBacteria; ACA37842; ACA37842; Bsph_0211.
DR KEGG; lsp:Bsph_0211; -.
DR HOGENOM; CLU_061495_2_0_9; -.
DR OMA; EFCYKND; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000002164; 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.
FT CHAIN 1..236
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_1000095993"
SQ SEQUENCE 236 AA; 26424 MW; BADA6F628935D0DC CRC64;
MTKGQLLYEG KAKKLYTTEE PNVLLVEYKD SATAFNGEKK EEIEGKGILN NRITSLIFEK
LQGNGIASHF VKQLSDTQQL VRKVDIIPIE VVVRNIVAGS LAKRIGLEEG TPLKRPIVEF
YYKDDELGDP FITTEHIDVL ELATSAEVSA IYDKALAINK VLQPIFADVN VTLIDFKLEF
GRDADGHVLL ADEISPDTCR LWDATTKQKL DKDVFRRDLG NLTEVYTIIL SRLGGK