ID   ULAE_ECO45              Reviewed;         284 AA.
AC   B7MLK2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=L-ribulose-5-phosphate 3-epimerase UlaE {ECO:0000255|HAMAP-Rule:MF_01951};
DE            EC=5.1.3.22 {ECO:0000255|HAMAP-Rule:MF_01951};
DE   AltName: Full=L-ascorbate utilization protein E {ECO:0000255|HAMAP-Rule:MF_01951};
DE   AltName: Full=L-xylulose-5-phosphate 3-epimerase {ECO:0000255|HAMAP-Rule:MF_01951};
GN   Name=ulaE {ECO:0000255|HAMAP-Rule:MF_01951}; OrderedLocusNames=ECS88_4783;
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Catalyzes the isomerization of L-xylulose-5-phosphate to L-
CC       ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate
CC       utilization. {ECO:0000255|HAMAP-Rule:MF_01951}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ribulose 5-phosphate = L-xylulose 5-phosphate;
CC         Xref=Rhea:RHEA:18497, ChEBI:CHEBI:57829, ChEBI:CHEBI:58226;
CC         EC=5.1.3.22; Evidence={ECO:0000255|HAMAP-Rule:MF_01951};
CC   -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose 5-
CC       phosphate from L-ascorbate: step 3/4. {ECO:0000255|HAMAP-
CC       Rule:MF_01951}.
CC   -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR.
CC       {ECO:0000255|HAMAP-Rule:MF_01951}.
CC   -!- SIMILARITY: Belongs to the L-ribulose-5-phosphate 3-epimerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01951}.
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DR   EMBL; CU928161; CAR05932.1; -; Genomic_DNA.
DR   RefSeq; WP_000949496.1; NC_011742.1.
DR   AlphaFoldDB; B7MLK2; -.
DR   SMR; B7MLK2; -.
DR   EnsemblBacteria; CAR05932; CAR05932; ECS88_4783.
DR   KEGG; ecz:ECS88_4783; -.
DR   HOGENOM; CLU_082738_0_0_6; -.
DR   OMA; QAGMGHI; -.
DR   UniPathway; UPA00263; UER00379.
DR   Proteomes; UP000000747; Chromosome.
DR   GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:InterPro.
DR   GO; GO:0034015; F:L-ribulose-5-phosphate 3-epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01951; UlaE; 1.
DR   InterPro; IPR004560; L-Ru-5P_3-Epase.
DR   InterPro; IPR023492; L-Ru-5P_3-Epase_Enterobacteria.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   SUPFAM; SSF51658; SSF51658; 1.
DR   TIGRFAMs; TIGR00542; hxl6Piso_put; 1.
PE   3: Inferred from homology;
KW   Isomerase.
FT   CHAIN           1..284
FT                   /note="L-ribulose-5-phosphate 3-epimerase UlaE"
FT                   /id="PRO_1000188821"
SQ   SEQUENCE   284 AA;  32069 MW;  0AA720920722A5A3 CRC64;
     MLSKQIPLGI YEKALPAGEC WLERLQLAKT LGFDFVEMSV DETDDRLSRL DWSREQRLAL
     VNAIVETGVR VPSMCLSAHR RFPLGSEDDA VRAQGLEIMR KAIQFAQDVG IRVIQLAGYD
     VYYQEANNET RRRFRDGLKE SVEMASRAQV TLAMEIMDYP LMNSISKALG YAHYFNNPWF
     QLYPDIGNLS AWDNDVQMEL QAGIGHIVAV HVKDTKPGVF KNVPFGEGVV DFERCFETLK
     QSGYCGPYLI EMWSETAEDP AAEVAKARDW VKARMAKAGM VEAA