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N5-carboxyaminoimidazole ribonucleotide mutase (N5-CAIR mutase) (EC 5.4.99.18) (5-(carboxyamino)imidazole ribonucleotide mutase)

 PURE_ECOLI              Reviewed;         169 AA.
P0AG18; P09028; Q2MBQ6;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 101.
RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000305};
Short=N5-CAIR mutase {ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000305};
EC=5.4.99.18 {ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000269|PubMed:10074353, ECO:0000269|PubMed:8117684};
AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000305};
Name=purE {ECO:0000255|HAMAP-Rule:MF_01929};
OrderedLocusNames=b0523, JW0512;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=2464576; DOI=10.1128/jb.171.1.205-212.1989;
Tiedeman A.A., Keyhani J., Kamholz J., Daum H.A. III, Gots J.S.,
Smith J.M.;
"Nucleotide sequence analysis of the purEK operon encoding 5'-
phosphoribosyl-5-aminoimidazole carboxylase of Escherichia coli K-
12.";
J. Bacteriol. 171:205-212(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2644189; DOI=10.1128/jb.171.1.198-204.1989;
Watanabe W., Sampei G., Aiba A., Mizobuchi K.;
"Identification and sequence analysis of Escherichia coli purE and
purK genes encoding 5'-phosphoribosyl-5-amino-4-imidazole carboxylase
for de novo purine biosynthesis.";
J. Bacteriol. 171:198-204(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
PROTEIN SEQUENCE OF 2-11.
PubMed=1534690; DOI=10.1021/bi00136a016;
Meyer E., Leonard N.J., Bhat B., Stubbe J., Smith J.M.;
"Purification and characterization of the purE, purK, and purC gene
products: identification of a previously unrecognized energy
requirement in the purine biosynthetic pathway.";
Biochemistry 31:5022-5032(1992).
[7]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
PubMed=8117684; DOI=10.1021/bi00174a038;
Mueller E.J., Meyer E., Rudolph J., Davisson V.J., Stubbe J.;
"N5-carboxyaminoimidazole ribonucleotide: evidence for a new
intermediate and two new enzymatic activities in the de novo purine
biosynthetic pathway of Escherichia coli.";
Biochemistry 33:2269-2278(1994).
[8]
CATALYTIC ACTIVITY, AND REACTION MECHANISM.
PubMed=10074353; DOI=10.1021/bi9827159;
Meyer E., Kappock T.J., Osuji C., Stubbe J.;
"Evidence for the direct transfer of the carboxylate of N5-
carboxyaminoimidazole ribonucleotide (N5-CAIR) to generate 4-carboxy-
5-aminoimidazole ribonucleotide catalyzed by Escherichia coli PurE, an
N5-CAIR mutase.";
Biochemistry 38:3012-3018(1999).
[9]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH
N5-CARBOXYAMINOIMIDAZOLE RIBONUCLEOTIDE, AND SUBUNIT.
PubMed=10574791; DOI=10.1016/S0969-2126(00)80029-5;
Mathews I.I., Kappock T.J., Stubbe J., Ealick S.E.;
"Crystal structure of Escherichia coli PurE, an unusual mutase in the
purine biosynthetic pathway.";
Structure 7:1395-1406(1999).
-!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole
ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole
ribonucleotide (CAIR). {ECO:0000255|HAMAP-Rule:MF_01929,
ECO:0000269|PubMed:8117684}.
-!- CATALYTIC ACTIVITY: 5-carboxyamino-1-(5-phospho-D-
ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-
carboxylate. {ECO:0000255|HAMAP-Rule:MF_01929,
ECO:0000269|PubMed:10074353, ECO:0000269|PubMed:8117684}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=140 uM for N5-CAIR {ECO:0000269|PubMed:8117684};
-!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-
amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2.
{ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000269|PubMed:8117684}.
-!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:10574791}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-909394, EBI-909394;
-!- SIMILARITY: Belongs to the AIR carboxylase family. Class I
subfamily. {ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000305}.
-!- CAUTION: Was originally thought to be the catalytic subunit of
phosphoribosylaminoimidazole carboxylase, with ATPase subunit
PurK. {ECO:0000305|PubMed:2464576}.
-----------------------------------------------------------------------
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EMBL; X12982; CAA31420.1; -; Genomic_DNA.
EMBL; M19657; AAA24449.1; -; Genomic_DNA.
EMBL; U82664; AAB40276.1; -; Genomic_DNA.
EMBL; U00096; AAC73625.1; -; Genomic_DNA.
EMBL; AP009048; BAE76300.1; -; Genomic_DNA.
PIR; JT0499; DEECPE.
RefSeq; NP_415056.1; NC_000913.3.
RefSeq; WP_001295318.1; NZ_LN832404.1.
PDB; 1D7A; X-ray; 2.50 A; A/B/C/D/L/M/N/O=8-167.
PDB; 1QCZ; X-ray; 1.50 A; A=1-169.
PDB; 2ATE; X-ray; 1.80 A; A=1-169.
PDB; 2NSH; X-ray; 1.80 A; A=1-169.
PDB; 2NSJ; X-ray; 2.31 A; A=1-169.
PDB; 2NSL; X-ray; 2.00 A; A=1-169.
PDBsum; 1D7A; -.
PDBsum; 1QCZ; -.
PDBsum; 2ATE; -.
PDBsum; 2NSH; -.
PDBsum; 2NSJ; -.
PDBsum; 2NSL; -.
ProteinModelPortal; P0AG18; -.
SMR; P0AG18; -.
BioGrid; 4261243; 17.
DIP; DIP-10610N; -.
IntAct; P0AG18; 11.
STRING; 316385.ECDH10B_0479; -.
SWISS-2DPAGE; P0AG18; -.
PaxDb; P0AG18; -.
PRIDE; P0AG18; -.
EnsemblBacteria; AAC73625; AAC73625; b0523.
EnsemblBacteria; BAE76300; BAE76300; BAE76300.
GeneID; 949031; -.
KEGG; ecj:JW0512; -.
KEGG; eco:b0523; -.
PATRIC; fig|1411691.4.peg.1755; -.
EchoBASE; EB0786; -.
EcoGene; EG10793; purE.
eggNOG; ENOG4108UM6; Bacteria.
eggNOG; COG0041; LUCA.
HOGENOM; HOG000034140; -.
InParanoid; P0AG18; -.
KO; K01588; -.
PhylomeDB; P0AG18; -.
BioCyc; EcoCyc:PURE-MONOMER; -.
BioCyc; MetaCyc:PURE-MONOMER; -.
BRENDA; 5.4.99.18; 2026.
UniPathway; UPA00074; UER00943.
EvolutionaryTrace; P0AG18; -.
PRO; PR:P0AG18; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.50.7700; -; 1.
HAMAP; MF_01929; PurE_classI; 1.
InterPro; IPR033747; PurE_ClassI.
InterPro; IPR000031; PurE_dom.
InterPro; IPR024694; PurE_prokaryotes.
InterPro; IPR035893; PurE_sf.
Pfam; PF00731; AIRC; 1.
PIRSF; PIRSF001338; AIR_carboxylase; 1.
SMART; SM01001; AIRC; 1.
SUPFAM; SSF52255; SSF52255; 1.
TIGRFAMs; TIGR01162; purE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing; Isomerase;
Purine biosynthesis; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1534690}.
CHAIN 2 169 N5-carboxyaminoimidazole ribonucleotide
mutase.
/FTId=PRO_0000074973.
BINDING 16 16 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01929,
ECO:0000269|PubMed:10574791}.
BINDING 19 19 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01929,
ECO:0000269|PubMed:10574791}.
BINDING 46 46 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01929,
ECO:0000269|PubMed:10574791}.
STRAND 10 16 {ECO:0000244|PDB:1QCZ}.
HELIX 17 19 {ECO:0000244|PDB:1QCZ}.
HELIX 20 33 {ECO:0000244|PDB:1QCZ}.
STRAND 37 41 {ECO:0000244|PDB:1QCZ}.
TURN 44 46 {ECO:0000244|PDB:1QCZ}.
HELIX 48 57 {ECO:0000244|PDB:1QCZ}.
TURN 58 62 {ECO:0000244|PDB:1QCZ}.
STRAND 64 70 {ECO:0000244|PDB:1QCZ}.
HELIX 76 82 {ECO:0000244|PDB:1QCZ}.
STRAND 88 92 {ECO:0000244|PDB:1QCZ}.
TURN 96 100 {ECO:0000244|PDB:1QCZ}.
HELIX 101 108 {ECO:0000244|PDB:1QCZ}.
HELIX 123 138 {ECO:0000244|PDB:1QCZ}.
HELIX 142 160 {ECO:0000244|PDB:1QCZ}.
SEQUENCE 169 AA; 17780 MW; E8B745B8D86E7D0B CRC64;
MSSRNNPARV AIVMGSKSDW ATMQFAAEIF EILNVPHHVE VVSAHRTPDK LFSFAESAEE
NGYQVIIAGA GGAAHLPGMI AAKTLVPVLG VPVQSAALSG VDSLYSIVQM PRGIPVGTLA
IGKAGAANAA LLAAQILATH DKELHQRLND WRKAQTDEVL ENPDPRGAA


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