PUR7_ECOLI
ID PUR7_ECOLI Reviewed; 237 AA.
AC P0A7D7; P21155;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase;
DE EC=6.3.2.6 {ECO:0000269|PubMed:1534690};
DE AltName: Full=SAICAR synthetase;
GN Name=purC; OrderedLocusNames=b2476, JW2461;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12;
RX PubMed=2120198; DOI=10.1128/jb.172.10.6035-6041.1990;
RA Tiedemann A.A., Demarini D.J., Parker J., Smith J.M.;
RT "DNA sequence of the purC gene encoding 5'-phosphoribosyl-5-aminoimidazole-
RT 4-N-succinocarboxamide synthetase and organization of the dapA-purC region
RT of Escherichia coli K-12.";
RL J. Bacteriol. 172:6035-6041(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RC STRAIN=K12;
RX PubMed=1885529; DOI=10.1128/jb.173.17.5523-5531.1991;
RA Bouvier J., Pugsley A.P., Stragier P.;
RT "A gene for a new lipoprotein in the dapA-purC interval of the Escherichia
RT coli chromosome.";
RL J. Bacteriol. 173:5523-5531(1991).
RN [6]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=1534690; DOI=10.1021/bi00136a016;
RA Meyer E., Leonard N.J., Bhat B., Stubbe J., Smith J.M.;
RT "Purification and characterization of the purE, purK, and purC gene
RT products: identification of a previously unrecognized energy requirement in
RT the purine biosynthetic pathway.";
RL Biochemistry 31:5022-5032(1992).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
CC -!- FUNCTION: Converts 4-carboxy-5-aminoimidazole ribonucleotide (CAIR) to
CC 4-(N-succinylcarboxamide)-5-aminoimidazole ribonucleotide (SAICAR).
CC {ECO:0000269|PubMed:1534690}.
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:0000269|PubMed:1534690};
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 -!- SUBUNIT: Homotrimer.
CC -!- SIMILARITY: Belongs to the SAICAR synthetase family. {ECO:0000305}.
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DR EMBL; M33928; AAA24448.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75529.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16353.1; -; Genomic_DNA.
DR EMBL; X57402; CAA40662.1; -; Genomic_DNA.
DR PIR; C36146; C36146.
DR RefSeq; NP_416971.1; NC_000913.3.
DR RefSeq; WP_001295467.1; NZ_STEB01000011.1.
DR PDB; 2GQR; X-ray; 2.00 A; A/B=1-237.
DR PDB; 2GQS; X-ray; 2.05 A; A/B=1-237.
DR PDBsum; 2GQR; -.
DR PDBsum; 2GQS; -.
DR AlphaFoldDB; P0A7D7; -.
DR SMR; P0A7D7; -.
DR BioGRID; 4261983; 44.
DR DIP; DIP-35900N; -.
DR IntAct; P0A7D7; 17.
DR STRING; 511145.b2476; -.
DR SWISS-2DPAGE; P0A7D7; -.
DR jPOST; P0A7D7; -.
DR PaxDb; P0A7D7; -.
DR PRIDE; P0A7D7; -.
DR EnsemblBacteria; AAC75529; AAC75529; b2476.
DR EnsemblBacteria; BAA16353; BAA16353; BAA16353.
DR GeneID; 67416868; -.
DR GeneID; 946957; -.
DR KEGG; ecj:JW2461; -.
DR KEGG; eco:b2476; -.
DR PATRIC; fig|1411691.4.peg.4263; -.
DR EchoBASE; EB0784; -.
DR eggNOG; COG0152; Bacteria.
DR HOGENOM; CLU_061495_2_1_6; -.
DR InParanoid; P0A7D7; -.
DR OMA; EFCYKND; -.
DR PhylomeDB; P0A7D7; -.
DR BioCyc; EcoCyc:SAICARSYN-MON; -.
DR BioCyc; MetaCyc:SAICARSYN-MON; -.
DR BRENDA; 6.3.2.6; 2026.
DR UniPathway; UPA00074; UER00131.
DR EvolutionaryTrace; P0A7D7; -.
DR PRO; PR:P0A7D7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IDA:EcoCyc.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR CDD; cd01415; SAICAR_synt_PurC; 1.
DR HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR033934; SAICAR_synt_PurC.
DR InterPro; IPR001636; SAICAR_synth.
DR InterPro; IPR018236; SAICAR_synthetase_CS.
DR Pfam; PF01259; SAICAR_synt; 1.
DR TIGRFAMs; TIGR00081; purC; 1.
DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Ligase;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..237
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_0000100825"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:2GQR"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:2GQR"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:2GQR"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2GQR"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:2GQR"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:2GQS"
FT HELIX 46..63
FT /evidence="ECO:0007829|PDB:2GQR"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:2GQR"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:2GQR"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:2GQR"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:2GQR"
FT STRAND 112..122
FT /evidence="ECO:0007829|PDB:2GQR"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:2GQR"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:2GQR"
FT HELIX 145..168
FT /evidence="ECO:0007829|PDB:2GQR"
FT STRAND 171..183
FT /evidence="ECO:0007829|PDB:2GQR"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:2GQR"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:2GQR"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:2GQR"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:2GQR"
FT HELIX 221..232
FT /evidence="ECO:0007829|PDB:2GQR"
SQ SEQUENCE 237 AA; 26995 MW; E5D0E69E84E35C97 CRC64;
MQKQAELYRG KAKTVYSTEN PDLLVLEFRN DTSAGDGARI EQFDRKGMVN NKFNYFIMSK
LAEAGIPTQM ERLLSDTECL VKKLDMVPVE CVVRNRAAGS LVKRLGIEEG IELNPPLFDL
FLKNDAMHDP MVNESYCETF GWVSKENLAR MKELTYKAND VLKKLFDDAG LILVDFKLEF
GLYKGEVVLG DEFSPDGSRL WDKETLEKMD KDRFRQSLGG LIEAYEAVAR RLGVQLD
