PUR7_ALISL
ID PUR7_ALISL Reviewed; 367 AA.
AC B6EMJ7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=VSAL_I1698;
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238;
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(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; FM178379; CAQ79383.1; -; Genomic_DNA.
DR RefSeq; WP_012550315.1; NC_011312.1.
DR AlphaFoldDB; B6EMJ7; -.
DR SMR; B6EMJ7; -.
DR STRING; 316275.VSAL_I1698; -.
DR EnsemblBacteria; CAQ79383; CAQ79383; VSAL_I1698.
DR KEGG; vsa:VSAL_I1698; -.
DR eggNOG; COG0152; Bacteria.
DR HOGENOM; CLU_064197_0_0_6; -.
DR OMA; QKARPVM; -.
DR OrthoDB; 1345271at2; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000001730; Chromosome 1.
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_1000117822"
SQ SEQUENCE 367 AA; 41500 MW; AF55050355A74156 CRC64;
MSLSEQVLAV NDDLPIRTDK PVHSGKVRSV YWLTEEDSRR LIKEKGYNVA PDAPLAIMVI
SDRISAFDCI WHGEGGLKGI PGKGAALNAI SNHWFQLFKD NNLADSHILD IPHPFVWIVQ
KAKPVMIEAI CRQYITGSMW RAYTNGEREF CGIQIPERLE KDEELADLLL TPSTKGVLKG
IEGVSEVDDV NITRKDIENN FSAFNFSSIE DIALYEKLLK EGFAVISKAL NDIDQIFVDT
KFEFGYVNDA QGNEKLIYMD EVGTPDSSRI WDKNAYRSGH IIENSKEGFR QFLLNHFPEP
DILLNKNRMD ERFALATENS LPLEAMMDLS KTYLDIAAKI TGAPIMLSDN PKAEIIKVLK
EQYQLVD
