PUR7_GEODF
ID PUR7_GEODF Reviewed; 296 AA.
AC B9M5S1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=Geob_3487;
OS Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS daltonii).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=316067;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22248 / JCM 15807 / FRC-32;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Kostka J., Richardson P.;
RT "Complete sequence of Geobacter sp. FRC-32.";
RL Submitted (JAN-2009) 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; CP001390; ACM21830.1; -; Genomic_DNA.
DR RefSeq; WP_012648558.1; NC_011979.1.
DR AlphaFoldDB; B9M5S1; -.
DR SMR; B9M5S1; -.
DR STRING; 316067.Geob_3487; -.
DR EnsemblBacteria; ACM21830; ACM21830; Geob_3487.
DR KEGG; geo:Geob_3487; -.
DR eggNOG; COG0152; Bacteria.
DR HOGENOM; CLU_045637_0_0_7; -.
DR OMA; TKFEFGF; -.
DR OrthoDB; 1345271at2; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000007721; 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; IPR001636; SAICAR_synth.
DR Pfam; PF01259; SAICAR_synt; 1.
DR TIGRFAMs; TIGR00081; purC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..296
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_1000122917"
SQ SEQUENCE 296 AA; 33315 MW; 9D3A648EFC68080A CRC64;
MSKLVLTTDF PDLKLAARGK VRDIYDLGET LLIVTTDRIS AFDVIMNEGI PDKGYVLTQI
SAFWFRQMED IIKNHIISTE VKDFPSACQK YADILEGRSM LVKKAKPLPA ECIVRGYISG
SGWKDYKATG SICGIKLPEG LKESDRLPQP IFTPSTKAEL GTHDENISFE KMVELCGKET
AEKVRDVTLK IYMKARDIAD TKGIIIADTK FEYGIYNGEL IIIDECMTPD SSRFWPKDSY
HPGGPQPSFD KQFLRDYLET LDWNKSAPAP PLPEEIVRKT GEKYMEALVK LTGKGK