PURE_ECOLI
ID PURE_ECOLI Reviewed; 169 AA.
AC P0AG18; P09028; Q2MBQ6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000305};
DE Short=N5-CAIR mutase {ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000305};
DE EC=5.4.99.18 {ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000269|PubMed:10074353, ECO:0000269|PubMed:8117684};
DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000305};
GN Name=purE {ECO:0000255|HAMAP-Rule:MF_01929};
GN OrderedLocusNames=b0523, JW0512;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2464576; DOI=10.1128/jb.171.1.205-212.1989;
RA Tiedeman A.A., Keyhani J., Kamholz J., Daum H.A. III, Gots J.S.,
RA Smith J.M.;
RT "Nucleotide sequence analysis of the purEK operon encoding 5'-
RT phosphoribosyl-5-aminoimidazole carboxylase of Escherichia coli K-12.";
RL J. Bacteriol. 171:205-212(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2644189; DOI=10.1128/jb.171.1.198-204.1989;
RA Watanabe W., Sampei G., Aiba A., Mizobuchi K.;
RT "Identification and sequence analysis of Escherichia coli purE and purK
RT genes encoding 5'-phosphoribosyl-5-amino-4-imidazole carboxylase for de
RT novo purine biosynthesis.";
RL J. Bacteriol. 171:198-204(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 2-11.
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RX PubMed=8117684; DOI=10.1021/bi00174a038;
RA Mueller E.J., Meyer E., Rudolph J., Davisson V.J., Stubbe J.;
RT "N5-carboxyaminoimidazole ribonucleotide: evidence for a new intermediate
RT and two new enzymatic activities in the de novo purine biosynthetic pathway
RT of Escherichia coli.";
RL Biochemistry 33:2269-2278(1994).
RN [8]
RP CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX PubMed=10074353; DOI=10.1021/bi9827159;
RA Meyer E., Kappock T.J., Osuji C., Stubbe J.;
RT "Evidence for the direct transfer of the carboxylate of N5-
RT carboxyaminoimidazole ribonucleotide (N5-CAIR) to generate 4-carboxy-5-
RT aminoimidazole ribonucleotide catalyzed by Escherichia coli PurE, an N5-
RT CAIR mutase.";
RL Biochemistry 38:3012-3018(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH
RP N5-CARBOXYAMINOIMIDAZOLE RIBONUCLEOTIDE, AND SUBUNIT.
RX PubMed=10574791; DOI=10.1016/s0969-2126(00)80029-5;
RA Mathews I.I., Kappock T.J., Stubbe J., Ealick S.E.;
RT "Crystal structure of Escherichia coli PurE, an unusual mutase in the
RT purine biosynthetic pathway.";
RL Structure 7:1395-1406(1999).
CC -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole
CC ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide
CC (CAIR). {ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000269|PubMed:8117684}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate;
CC Xref=Rhea:RHEA:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:58730,
CC ChEBI:CHEBI:77657; EC=5.4.99.18; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01929, ECO:0000269|PubMed:10074353,
CC ECO:0000269|PubMed:8117684};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=140 uM for N5-CAIR {ECO:0000269|PubMed:8117684};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2.
CC {ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000269|PubMed:8117684}.
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:10574791}.
CC -!- INTERACTION:
CC P0AG18; P0AG18: purE; NbExp=2; IntAct=EBI-909394, EBI-909394;
CC -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the catalytic subunit of
CC phosphoribosylaminoimidazole carboxylase, with ATPase subunit PurK.
CC {ECO:0000305|PubMed:2464576}.
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DR EMBL; X12982; CAA31420.1; -; Genomic_DNA.
DR EMBL; M19657; AAA24449.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40276.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73625.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76300.1; -; Genomic_DNA.
DR PIR; JT0499; DEECPE.
DR RefSeq; NP_415056.1; NC_000913.3.
DR RefSeq; WP_001295318.1; NZ_STEB01000007.1.
DR PDB; 1D7A; X-ray; 2.50 A; A/B/C/D/L/M/N/O=8-167.
DR PDB; 1QCZ; X-ray; 1.50 A; A=1-169.
DR PDB; 2ATE; X-ray; 1.80 A; A=1-169.
DR PDB; 2NSH; X-ray; 1.80 A; A=1-169.
DR PDB; 2NSJ; X-ray; 2.31 A; A=1-169.
DR PDB; 2NSL; X-ray; 2.00 A; A=1-169.
DR PDBsum; 1D7A; -.
DR PDBsum; 1QCZ; -.
DR PDBsum; 2ATE; -.
DR PDBsum; 2NSH; -.
DR PDBsum; 2NSJ; -.
DR PDBsum; 2NSL; -.
DR AlphaFoldDB; P0AG18; -.
DR SMR; P0AG18; -.
DR BioGRID; 4261243; 17.
DR DIP; DIP-10610N; -.
DR IntAct; P0AG18; 11.
DR STRING; 511145.b0523; -.
DR SWISS-2DPAGE; P0AG18; -.
DR jPOST; P0AG18; -.
DR PaxDb; P0AG18; -.
DR PRIDE; P0AG18; -.
DR EnsemblBacteria; AAC73625; AAC73625; b0523.
DR EnsemblBacteria; BAE76300; BAE76300; BAE76300.
DR GeneID; 66671182; -.
DR GeneID; 949031; -.
DR KEGG; ecj:JW0512; -.
DR KEGG; eco:b0523; -.
DR PATRIC; fig|1411691.4.peg.1755; -.
DR EchoBASE; EB0786; -.
DR eggNOG; COG0041; Bacteria.
DR HOGENOM; CLU_094982_2_2_6; -.
DR InParanoid; P0AG18; -.
DR OMA; SNSIDGW; -.
DR PhylomeDB; P0AG18; -.
DR BioCyc; EcoCyc:PURE-MON; -.
DR BioCyc; MetaCyc:PURE-MON; -.
DR BRENDA; 5.4.99.18; 2026.
DR SABIO-RK; P0AG18; -.
DR UniPathway; UPA00074; UER00943.
DR EvolutionaryTrace; P0AG18; -.
DR PRO; PR:P0AG18; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01929; PurE_classI; 1.
DR InterPro; IPR033747; PurE_ClassI.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR024694; PurE_prokaryotes.
DR Pfam; PF00731; AIRC; 1.
DR PIRSF; PIRSF001338; AIR_carboxylase; 1.
DR SMART; SM01001; AIRC; 1.
DR TIGRFAMs; TIGR01162; purE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isomerase; Purine biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1534690"
FT CHAIN 2..169
FT /note="N5-carboxyaminoimidazole ribonucleotide mutase"
FT /id="PRO_0000074973"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929,
FT ECO:0000269|PubMed:10574791"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929,
FT ECO:0000269|PubMed:10574791"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929,
FT ECO:0000269|PubMed:10574791"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:1QCZ"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1QCZ"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:1QCZ"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1QCZ"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1QCZ"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:1QCZ"
FT TURN 58..62
FT /evidence="ECO:0007829|PDB:1QCZ"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1QCZ"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:1QCZ"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:1QCZ"
FT TURN 96..100
FT /evidence="ECO:0007829|PDB:1QCZ"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:1QCZ"
FT HELIX 123..138
FT /evidence="ECO:0007829|PDB:1QCZ"
FT HELIX 142..160
FT /evidence="ECO:0007829|PDB:1QCZ"
SQ SEQUENCE 169 AA; 17780 MW; E8B745B8D86E7D0B CRC64;
MSSRNNPARV AIVMGSKSDW ATMQFAAEIF EILNVPHHVE VVSAHRTPDK LFSFAESAEE
NGYQVIIAGA GGAAHLPGMI AAKTLVPVLG VPVQSAALSG VDSLYSIVQM PRGIPVGTLA
IGKAGAANAA LLAAQILATH DKELHQRLND WRKAQTDEVL ENPDPRGAA
