ULAE_ECOL5
ID ULAE_ECOL5 Reviewed; 284 AA.
AC Q0T9J6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=ECP_4442;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG72383.1; -; Genomic_DNA.
DR RefSeq; WP_000949498.1; NC_008253.1.
DR AlphaFoldDB; Q0T9J6; -.
DR SMR; Q0T9J6; -.
DR STRING; 362663.ECP_4442; -.
DR EnsemblBacteria; ABG72383; ABG72383; ECP_4442.
DR KEGG; ecp:ECP_4442; -.
DR HOGENOM; CLU_082738_0_0_6; -.
DR OMA; QAGMGHI; -.
DR UniPathway; UPA00263; UER00379.
DR Proteomes; UP000009182; 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_1000070633"
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
