(data stored in ACNUC7421 zone)

SWISSPROT: A0KEX5_AERHH

ID   A0KEX5_AERHH            Unreviewed;       167 AA.
AC   A0KEX5;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 88.
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-2 {ECO:0000313|EMBL:ABK39569.1};
GN   Synonyms=purE {ECO:0000256|HAMAP-Rule:MF_01929};
GN   OrderedLocusNames=AHA_0263 {ECO:0000313|EMBL:ABK39569.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39569.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK39569.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK39569.1; -; Genomic_DNA.
DR   RefSeq; WP_011704271.1; NC_008570.1.
DR   RefSeq; YP_854791.1; NC_008570.1.
DR   STRING; 380703.AHA_0263; -.
DR   EnsemblBacteria; ABK39569; ABK39569; AHA_0263.
DR   GeneID; 4490194; -.
DR   KEGG; aha:AHA_0263; -.
DR   PATRIC; fig|380703.7.peg.250; -.
DR   eggNOG; ENOG4108UM6; Bacteria.
DR   eggNOG; COG0041; LUCA.
DR   HOGENOM; HOG000034140; -.
DR   KO; K01588; -.
DR   OMA; SNSIDGW; -.
DR   BioCyc; AHYD380703:G1G7B-264-MONOMER; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; A0KEX5.
DR   SWISS-2DPAGE; A0KEX5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01929,
KW   ECO:0000256|PIRNR:PIRNR001338}; Lyase {ECO:0000313|EMBL:ABK39569.1};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01929,
KW   ECO:0000256|PIRNR:PIRNR001338};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756}.
FT   DOMAIN        4    155       AIRC. {ECO:0000259|SMART:SM01001}.
FT   BINDING      12     12       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01929, ECO:0000256|PIRSR:PIRSR001338-
FT                                1}.
FT   BINDING      15     15       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01929, ECO:0000256|PIRSR:PIRSR001338-
FT                                1}.
FT   BINDING      42     42       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01929, ECO:0000256|PIRSR:PIRSR001338-
FT                                1}.
SQ   SEQUENCE   167 AA;  17076 MW;  9BE60E8CAC89C22D CRC64;
     MNKPFVAVLM GSDSDFPVMQ TTLEVLKSFD IAVEVKVTSA HRTPAATHQY VTDAEARGCK
     VFICAAGLAA HLAGAVAGIT TRPVIGVPID GGPLKGLDAL LSTVQMPGGV PVATVAIGKA
     GAKNAGYLAA QMLAVADDEL AAKVQAERQK NADEVLAKDA ALQALLK
//

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