ID   ULAE_ECOUT              Reviewed;         284 AA.
AC   Q1R363;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=L-ribulose-5-phosphate 3-epimerase ulaE;
DE            EC=5.1.3.22;
DE   AltName: Full=L-xylulose-5-phosphate 3-epimerase;
DE   AltName: Full=L-ascorbate utilization protein E;
GN   Name=ulaE; OrderedLocusNames=UTI89_C4797;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Catalyzes the isomerization of L-xylulose-5-phosphate to
CC       L-ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate
CC       utilization (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-ribulose 5-phosphate = L-xylulose 5-
CC       phosphate.
CC   -!- PATHWAY: Cofactor degradation; L-ascorbic acid degradation; D-
CC       xylulose 5-phosphate from L-ascorbic acid: step 3/4.
CC   -!- INDUCTION: Induced by L-ascorbate. Repressed by ulaR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the HUMPI family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000243; ABE10201.1; -; Genomic_DNA.
DR   RefSeq; YP_543732.1; -.
DR   GeneID; 3989836; -.
DR   GenomeReviews; CP000243_GR; UTI89_C4797.
DR   KEGG; eci:UTI89_C4797; -.
DR   HOGENOM; Q1R363; -.
DR   OMA; Q1R363; VVKARDW.
DR   BioCyc; ECOL364106:UTI89_C4797-MON; -.
DR   GO; GO:0016861; F:intramolecular oxidoreductase activity, int...; IEA:InterPro.
DR   GO; GO:0034015; F:L-ribulose-5-phosphate 3-epimerase activity; IEA:HAMAP.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0019852; P:L-ascorbic acid metabolic process; IEA:HAMAP.
DR   HAMAP; MF_01951; -; 1.
DR   InterPro; IPR004560; Hxl6Piso_put.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   InterPro; IPR012307; Xyl_isomerase-typ_TIM-brl.
DR   Gene3D; G3DSA:3.20.20.150; Xyl_isomerase-like_TIM-brl; 1.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   TIGRFAMs; TIGR00542; hxl6Piso_put; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Isomerase.
FT   CHAIN         1    284       L-ribulose-5-phosphate 3-epimerase ulaE.
FT                                /FTId=PRO_1000070634.
SQ   SEQUENCE   284 AA;  32035 MW;  31CA9644DC4A8529 CRC64;
     MLSKQIPLGI YEKALPAGEC WLERLQLAKT LGFDFVEMSV DETDDRLSRL DWSREQRLAL
     VNAIVETGVR VPSMCLSAHR RFPLGSEDDA VRAQGLEIMR KAIQFAQDVG IRVIQLAGYD
     VYYQEANNET RRRFRDGLKE SVEMASRAQV TLAMEIMDYP LMNSISKALG YAHYLNNPWF
     QLYPDIGNLS AWDNDVQMEL QAGIGHIVAV HVKDTKPGVF KNVPFGEGVV DFERCFETLK
     QSGYCGPYLI EMWSETAEDP AAEVAKARDW VKARMAKAGM VEAA
//