PUR7_SHEHH
ID PUR7_SHEHH Reviewed; 367 AA.
AC B0TQY6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=Shal_1816;
OS Shewanella halifaxensis (strain HAW-EB4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=458817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000931; ABZ76381.1; -; Genomic_DNA.
DR RefSeq; WP_012276913.1; NC_010334.1.
DR AlphaFoldDB; B0TQY6; -.
DR SMR; B0TQY6; -.
DR STRING; 458817.Shal_1816; -.
DR EnsemblBacteria; ABZ76381; ABZ76381; Shal_1816.
DR KEGG; shl:Shal_1816; -.
DR eggNOG; COG0152; Bacteria.
DR HOGENOM; CLU_064197_0_0_6; -.
DR OMA; QKARPVM; -.
DR OrthoDB; 1345271at2; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000001317; 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 HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR014106; SAICAR_synthase_Vibrio-typ.
DR Pfam; PF01259; SAICAR_synt; 1.
DR TIGRFAMs; TIGR02735; purC_vibrio; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..367
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_1000117849"
SQ SEQUENCE 367 AA; 41400 MW; 9ED18E51BC26A8C7 CRC64;
MNLADKVLVV NDNLPIRTNK PVHSGKVRSV YWLTEEDSAR LIKDKGYDVP ADAPLAIMVI
SDRISAFDCV WQGENGLNGV PGKGTALNAI SNHWFKLFKD KGLADSHILD IPHPLVWIVQ
KARPVMIEAI ARQYITGSMW RSYTKGEREF CGITIPEGLE KDQKLPELLI TPSTKGVLTG
LEGVPEADDV NVSRSDIERH VEGFNFTKLA DIDLYEKLLK EGFDVISDAL AEHDQVFVDT
KFEFGYVNDA AGNEKLIYMD EVGTPDSSRI WDGSSHRDGK IIEQSKEGFR QWLLNHFPDS
DILLNKNRME ERFALARDNK LPESVMMDIS NTYVGIAEKV IGSKLKISEN PKQEIIDILR
EEYQLIV