(data stored in SCRATCH zone)

SWISSPROT: C8U1D2_ECO10

ID   C8U1D2_ECO10            Unreviewed;       231 AA.
AC   C8U1D2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 51.
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:BAI28940.1};
GN   OrderedLocusNames=ECO103_0062 {ECO:0000313|EMBL:BAI28940.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28940.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28940.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(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; AP010958; BAI28940.1; -; Genomic_DNA.
DR   RefSeq; WP_000888642.1; NC_013353.1.
DR   EnsemblBacteria; BAI28940; BAI28940; ECO103_0062.
DR   KEGG; eoh:ECO103_0062; -.
DR   HOGENOM; HOG000218183; -.
DR   KO; K03077; -.
DR   OMA; IFGTTHA; -.
DR   BioCyc; ECOL585395:ECO103_RS00315-MONOMER; -.
DR   UniPathway; UPA00145; UER00567.
DR   Proteomes; UP000000959; 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; C8U1D2.
DR   SWISS-2DPAGE; C8U1D2.
KW   Arabinose catabolism {ECO:0000256|HAMAP-Rule:MF_00989};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00989};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
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;  25446 MW;  404620B2ED962274 CRC64;
     MLEDLKRLVL EANLALPKHN LVTLTWGNVS AVDRERGVFV IKPSGVDYSV MTADDMVVVS
     IATGEVVEGT KKPSSDTPTH RLLYQAFPSI GGIVHTHSRH ATIWAQAGQS IPATGTTHAD
     YFYGTIPCTR KMTDAEINGE YEWETGNVIV ETFEKQGIDA AQMPGVLVHS HGPFAWGKNA
     EDAVHNAIVL EEVAYMGIFC RQLAPQLPDM QQTLLDKHYL RKHGAKAYYG Q
//

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