(data stored in ACNUC7421 zone)

SWISSPROT: B7UIA7_ECO27

ID   B7UIA7_ECO27            Unreviewed;       231 AA.
AC   B7UIA7;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 52.
DE   RecName: Full=L-ribulose-5-phosphate 4-epimerase {ECO:0000256|HAMAP-Rule:MF_00989};
DE            EC=5.1.3.4 {ECO:0000256|HAMAP-Rule:MF_00989};
DE   AltName: Full=Phosphoribulose isomerase {ECO:0000256|HAMAP-Rule:MF_00989};
GN   Name=araD {ECO:0000256|HAMAP-Rule:MF_00989,
GN   ECO:0000313|EMBL:CAS07610.1};
GN   OrderedLocusNames=E2348C_0062 {ECO:0000313|EMBL:CAS07610.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07610.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07610.1, 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: Involved in the degradation of L-arabinose. Catalyzes
CC       the interconversion of L-ribulose 5-phosphate (LRu5P) and D-
CC       xylulose 5-phosphate (D-Xu5P) via a retroaldol/aldol mechanism
CC       (carbon-carbon bond cleavage analogous to a class II aldolase
CC       reaction). {ECO:0000256|HAMAP-Rule:MF_00989}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ribulose 5-phosphate = D-xylulose 5-phosphate;
CC         Xref=Rhea:RHEA:22368, ChEBI:CHEBI:57737, ChEBI:CHEBI:58226;
CC         EC=5.1.3.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00989};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00989};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00989};
CC   -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC       ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial
CC       route): step 3/3. {ECO:0000256|HAMAP-Rule:MF_00989}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00989}.
CC   -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00989}.
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DR   EMBL; FM180568; CAS07610.1; -; Genomic_DNA.
DR   RefSeq; WP_000888696.1; NC_011601.1.
DR   EnsemblBacteria; CAS07610; CAS07610; E2348C_0062.
DR   KEGG; ecg:E2348C_0062; -.
DR   HOGENOM; HOG000218183; -.
DR   KO; K03077; -.
DR   OMA; IFGTTHA; -.
DR   BioCyc; ECOL574521:E2348C_RS00320-MONOMER; -.
DR   UniPathway; UPA00145; UER00567.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.225.10; -; 1.
DR   HAMAP; MF_00989; AraD_entero; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR   InterPro; IPR004661; AraD.
DR   InterPro; IPR033748; AraD_entero.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   SMART; SM01007; Aldolase_II; 1.
DR   SUPFAM; SSF53639; SSF53639; 1.
DR   TIGRFAMs; TIGR00760; araD; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UIA7.
DR   SWISS-2DPAGE; B7UIA7.
KW   Arabinose catabolism {ECO:0000256|HAMAP-Rule:MF_00989};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00989};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00989};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00989};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00989}.
FT   DOMAIN        7    198       Aldolase_II. {ECO:0000259|SMART:SM01007}.
FT   REGION       27     28       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00989}.
FT   REGION       44     45       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00989}.
FT   REGION       74     75       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00989}.
FT   ACT_SITE    120    120       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00989}.
FT   ACT_SITE    229    229       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00989}.
FT   METAL        76     76       Zinc. {ECO:0000256|HAMAP-Rule:MF_00989}.
FT   METAL        95     95       Zinc; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00989}.
FT   METAL        97     97       Zinc; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00989}.
FT   METAL       171    171       Zinc; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00989}.
SQ   SEQUENCE   231 AA;  25423 MW;  DA2D315139DBBFB1 CRC64;
     MLEDLKRQVL EANLALPKHN LVTLTWGNVS AVDRGRGVLV IKPSGVDYSI MTADDMVVVS
     IETGEVVEGT KKPSSDTPTH RLLYQAFPSI GGIVHTHSRH ATIWAQAGQS IPATGTTHAD
     YFYGPIPCTR KMTDAEINGE YEWETGNVIV ETFEKQGIDA AQMPGVLVHS HGPFAWGKNA
     EDAVHNAIVL EEVAYMGIFC RQLAPQLPDM QQTLLDKHYL RKHGAKAYYG Q
//

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