(data stored in ACNUC7421 zone)

SWISSPROT: B7UKK0_ECO27

ID   B7UKK0_ECO27            Unreviewed;       169 AA.
AC   B7UKK0;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338};
DE            Short=N5-CAIR mutase {ECO:0000256|HAMAP-Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338};
DE            EC=5.4.99.18 {ECO:0000256|HAMAP-Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338};
DE   AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929};
GN   Name=purE {ECO:0000256|HAMAP-Rule:MF_01929,
GN   ECO:0000313|EMBL:CAS08004.1};
GN   OrderedLocusNames=E2348C_0456 {ECO:0000313|EMBL:CAS08004.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08004.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08004.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole
CC       ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole
CC       ribonucleotide (CAIR). {ECO:0000256|HAMAP-Rule:MF_01929,
CC       ECO:0000256|PIRNR:PIRNR001338}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) =
CC         5-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:0000256|HAMAP-
CC         Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2.
CC       {ECO:0000256|HAMAP-Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338}.
CC   -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01929}.
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DR   EMBL; FM180568; CAS08004.1; -; Genomic_DNA.
DR   RefSeq; WP_001298348.1; NC_011601.1.
DR   EnsemblBacteria; CAS08004; CAS08004; E2348C_0456.
DR   KEGG; ecg:E2348C_0456; -.
DR   HOGENOM; HOG000034140; -.
DR   KO; K01588; -.
DR   OMA; SNSIDGW; -.
DR   BioCyc; ECOL574521:E2348C_RS02390-MONOMER; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.7700; -; 1.
DR   HAMAP; MF_01929; PurE_classI; 1.
DR   InterPro; IPR033747; PurE_ClassI.
DR   InterPro; IPR000031; PurE_dom.
DR   InterPro; IPR024694; PurE_prokaryotes.
DR   InterPro; IPR035893; PurE_sf.
DR   Pfam; PF00731; AIRC; 1.
DR   PIRSF; PIRSF001338; AIR_carboxylase; 1.
DR   SMART; SM01001; AIRC; 1.
DR   SUPFAM; SSF52255; SSF52255; 1.
DR   TIGRFAMs; TIGR01162; purE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UKK0.
DR   SWISS-2DPAGE; B7UKK0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01929,
KW   ECO:0000256|PIRNR:PIRNR001338};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01929,
KW   ECO:0000256|PIRNR:PIRNR001338}.
FT   DOMAIN        8    159       AIRC. {ECO:0000259|SMART:SM01001}.
FT   BINDING      16     16       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01929, ECO:0000256|PIRSR:PIRSR001338-
FT                                1}.
FT   BINDING      19     19       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01929, ECO:0000256|PIRSR:PIRSR001338-
FT                                1}.
FT   BINDING      46     46       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01929, ECO:0000256|PIRSR:PIRSR001338-
FT                                1}.
SQ   SEQUENCE   169 AA;  17794 MW;  E8B745B9031E7D0B CRC64;
     MSSRNNPARV AIVMGSKSDW ATMQFAAEIF EILNVPHHVE VVSAHRTPDK LFSFAESAEE
     NGYQVIIAGA GGAAHLPGMI AAKTLVPVLG VPVQSAALSG VDSLYSIVQM PRGIPVGTLA
     IGKAGAANAA LLAAQILATH DKELHQRLNE WRKAQTDEVL ENPDPRGAA
//

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