(data stored in SCRATCH zone)

SWISSPROT: Q8XA08_ECO57

ID   Q8XA08_ECO57            Unreviewed;       231 AA.
AC   Q8XA08; Q7AHS2;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 106.
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:AAG54365.1};
GN   OrderedLocusNames=ECs0065 {ECO:0000313|EMBL:BAB33488.1}, Z0069
GN   {ECO:0000313|EMBL:AAG54365.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|Proteomes:UP000002519};
RN   [1] {ECO:0000313|EMBL:BAB33488.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558}, and Sakai
RC   {ECO:0000313|EMBL:BAB33488.1};
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [2] {ECO:0000313|EMBL:AAG54365.1, ECO:0000313|Proteomes:UP000002519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EDL933 {ECO:0000313|EMBL:AAG54365.1}, and O157:H7 / EDL933 /
RC   ATCC 700927 / EHEC {ECO:0000313|Proteomes:UP000002519};
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G.III., Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
CC   -!- CATALYTIC ACTIVITY: L-ribulose 5-phosphate = D-xylulose 5-
CC       phosphate. {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; AE005174; AAG54365.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33488.1; -; Genomic_DNA.
DR   PIR; A85488; A85488.
DR   PIR; A90637; A90637.
DR   RefSeq; NP_308092.1; NC_002695.1.
DR   RefSeq; WP_000888654.1; NZ_MWVM01000003.1.
DR   ProteinModelPortal; Q8XA08; -.
DR   STRING; 155864.Z0069; -.
DR   EnsemblBacteria; AAG54365; AAG54365; Z0069.
DR   EnsemblBacteria; BAB33488; BAB33488; BAB33488.
DR   GeneID; 913465; -.
DR   KEGG; ece:Z0069; -.
DR   KEGG; ecs:ECs0065; -.
DR   PATRIC; fig|386585.9.peg.165; -.
DR   eggNOG; ENOG4107R0P; Bacteria.
DR   eggNOG; COG0235; LUCA.
DR   HOGENOM; HOG000218183; -.
DR   KO; K01786; -.
DR   UniPathway; UPA00145; UER00567.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.225.10; -; 1.
DR   HAMAP; MF_00989; AraD_entero; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
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; Q8XA08.
DR   SWISS-2DPAGE; Q8XA08.
KW   Arabinose catabolism {ECO:0000256|HAMAP-Rule:MF_00989};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00989};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558,
KW   ECO:0000313|Proteomes:UP000002519};
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   METAL        95     95       Zinc. {ECO:0000256|HAMAP-Rule:MF_00989}.
FT   METAL        97     97       Zinc. {ECO:0000256|HAMAP-Rule:MF_00989}.
FT   METAL       171    171       Zinc. {ECO:0000256|HAMAP-Rule:MF_00989}.
SQ   SEQUENCE   231 AA;  25503 MW;  15C2DF9F90E05A1B CRC64;
     MLEDLKRQVL EANLALPKHN LVTLTWGNVS AVDRERGVFV IKPSGVDYSI MTADDMVVVS
     IETGEVVEGA KKPSSDTPTH RLLYQAFPSI GGIVHTHSRH ATIWAQAGQS IPATGTTHAD
     YFYGTIPCTR KMTDAEINGE YEWETGNVIV ETFEKQGIDA AQMPGVLVHS HGPFAWGKNA
     EDAVHNAIVL EEVAYMGIFC RQLAPQLPDM QQTLLDKHYL RKHGAKAYYG Q
//

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