PUR7_SHEDO
ID PUR7_SHEDO Reviewed; 367 AA.
AC Q12JN5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=Sden_3063;
OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Shewanella denitrificans OS217.";
RL Submitted (MAR-2006) 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; CP000302; ABE56341.1; -; Genomic_DNA.
DR RefSeq; WP_011497487.1; NC_007954.1.
DR AlphaFoldDB; Q12JN5; -.
DR SMR; Q12JN5; -.
DR STRING; 318161.Sden_3063; -.
DR EnsemblBacteria; ABE56341; ABE56341; Sden_3063.
DR KEGG; sdn:Sden_3063; -.
DR eggNOG; COG0152; Bacteria.
DR HOGENOM; CLU_064197_0_0_6; -.
DR OMA; QKARPVM; -.
DR OrthoDB; 1345271at2; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000001982; 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 InterPro; IPR018236; SAICAR_synthetase_CS.
DR Pfam; PF01259; SAICAR_synt; 1.
DR TIGRFAMs; TIGR02735; purC_vibrio; 1.
DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..367
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_1000117847"
SQ SEQUENCE 367 AA; 40762 MW; B97AE14920D2FF0E CRC64;
MSLADSVLAV NNDLPIRTDK PVHSGKVRSV YWLTESDSRR LINDKGYKVP LDTPLAIMVI
SDRISAFDCI FHGEGGLQGI PGKGAALNAI SNHWFKLFAE QGLADSHILD IPHPFVWIVQ
KARPIKVEAI CRQYITGSMW RAYAKGEREF CGIRLPEGLK KDQKLPELII TPSTKGILTG
IPGVPAQDDV NISRQDIEAN YQAFGFESLS DIDLYETLLK DGFKVISDAL AQLDQVFVDT
KFEFGYVTDK NGQSKLIYMD EVGTPDSSRI WDGAAYRDSK IVENSKEGFR QFLLNHVADA
DVLLNKDRMP EREALARDNA LPLDAMMNVS RTYTGVAEKV TGKTITLAAN PKADIIAILK
KNYGLID
