ID   ULAE_ECOK1              Reviewed;         284 AA.
AC   A1AJA2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=Ecok1_42480;
GN   ORFNames=APECO1_2195;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ03742.1; -; Genomic_DNA.
DR   RefSeq; WP_000949496.1; NC_008563.1.
DR   AlphaFoldDB; A1AJA2; -.
DR   SMR; A1AJA2; -.
DR   EnsemblBacteria; ABJ03742; ABJ03742; APECO1_2195.
DR   KEGG; ecv:APECO1_2195; -.
DR   HOGENOM; CLU_082738_0_0_6; -.
DR   OMA; QAGMGHI; -.
DR   UniPathway; UPA00263; UER00379.
DR   Proteomes; UP000008216; 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_1000070632"
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