PUR7_ALIF1
ID PUR7_ALIF1 Reviewed; 367 AA.
AC Q5E4Q3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=VF_1498;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW85993.1; -; Genomic_DNA.
DR RefSeq; WP_011262080.1; NC_006840.2.
DR RefSeq; YP_204881.1; NC_006840.2.
DR AlphaFoldDB; Q5E4Q3; -.
DR SMR; Q5E4Q3; -.
DR STRING; 312309.VF_1498; -.
DR EnsemblBacteria; AAW85993; AAW85993; VF_1498.
DR KEGG; vfi:VF_1498; -.
DR PATRIC; fig|312309.11.peg.1515; -.
DR eggNOG; COG0152; Bacteria.
DR HOGENOM; CLU_064197_0_0_6; -.
DR OMA; QKARPVM; -.
DR OrthoDB; 1345271at2; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000000537; Chromosome I.
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;
KW Reference proteome.
FT CHAIN 1..367
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_1000117860"
SQ SEQUENCE 367 AA; 41599 MW; 884D7570EFE05C9C CRC64;
MSLSDQVLAV NDDLPIRTDK PVHSGKVRSV YWLTEEDSRR LIKEKGYNVA PDAPLAIMVI
SDRISAFDCI WHGEGDLKGI PGKGAALNAI SNHWFQLFKD NGLADSHILD IPHPFVWIVQ
KAKPVMIEAI CRQYITGSMW RAYTQGEREF CGITLPERLE KDEQLAELLL TPSTKGILKG
IDGVPEVDDV NITRKNIEDN YDKFNFSCIE DIATYEKLLK EGFAVIAKAL NKIDQIFVDT
KFEFGYVEDA QGNEKLIYMD EVGTPDSSRI WDTKAYRSGH IIENSKEGFR QFLLNHFPEP
DILLNKNRME ERFALAEENA LPLEAMMDLS KTYLDIAAKI TGAPITLSDN PKAEIIKVLK
EEYQLVD