(data stored in ACNUC7421 zone)

SWISSPROT: Q3Z4P2_SHISS

ID   Q3Z4P2_SHISS            Unreviewed;       169 AA.
AC   Q3Z4P2;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 92.
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:AAZ87270.1};
GN   OrderedLocusNames=SSON_0495 {ECO:0000313|EMBL:AAZ87270.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ87270.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ87270.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ87270.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000038; AAZ87270.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87270; AAZ87270; SSON_0495.
DR   KEGG; ssn:SSON_0495; -.
DR   HOGENOM; HOG000034140; -.
DR   KO; K01588; -.
DR   OMA; SNSIDGW; -.
DR   BioCyc; SSON300269:G1GL2-570-MONOMER; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000002529; 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; Q3Z4P2.
DR   SWISS-2DPAGE; Q3Z4P2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002529};
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;  17826 MW;  84AB35A3B465511B CRC64;
     MSSRNNPARV AIVMGSKSDW ATMQFAAEIF EILNVLHHVE VVSAHRTPDK LFSFAESAEE
     NGYQVIIAGA GGAAHLPGMI AAKTLVPVLG VPVQSAALSG VDSLYSIVQM PRGIPVGTLA
     IGKAGAANAA LLAAQILATH DKELHQRLND WRKAQTDEVL ENPDPRGTA
//

If you have problems or comments...

PBIL Back to PBIL home page