ULAE_ECOLI
ID ULAE_ECOLI Reviewed; 284 AA.
AC P39305; Q2M6A8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 145.
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}; Synonyms=sgaU, yjfW;
GN OrderedLocusNames=b4197, JW4155;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP DISCUSSION OF SEQUENCE.
RA Reizer J., Charbit A., Reizer A., Saier M.H. Jr.;
RT "Novel phosphotransferases system genes revealed by bacterial genome
RT analysis: operons encoding homologues of sugar-specific permease domains of
RT the phosphotransferase system and pentose catabolic enzymes.";
RL Genome Sci. Technol. 1:53-75(1996).
RN [5]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11741871; DOI=10.1128/jb.184.1.302-306.2002;
RA Yew W.S., Gerlt J.A.;
RT "Utilization of L-ascorbate by Escherichia coli K-12: assignments of
RT functions to products of the yjf-sga and yia-sgb operons.";
RL J. Bacteriol. 184:302-306(2002).
RN [6]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=12374842; DOI=10.1128/jb.184.21.6065-6068.2002;
RA Campos E., Aguilar J., Baldoma L., Badia J.;
RT "The gene yjfQ encodes the repressor of the yjfR-X regulon (ula), which is
RT involved in L-ascorbate metabolism in Escherichia coli.";
RL J. Bacteriol. 184:6065-6068(2002).
RN [7]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=14996803; DOI=10.1128/jb.186.6.1720-1728.2004;
RA Campos E., Baldoma L., Aguilar J., Badia J.;
RT "Regulation of expression of the divergent ulaG and ulaABCDEF operons
RT involved in L-ascorbate dissimilation in Escherichia coli.";
RL J. Bacteriol. 186:1720-1728(2004).
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 ECO:0000269|PubMed:11741871}.
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, ECO:0000269|PubMed:12374842,
CC ECO:0000269|PubMed:14996803}.
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; U14003; AAA97093.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77154.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78198.1; -; Genomic_DNA.
DR PIR; S56422; S56422.
DR RefSeq; NP_418618.1; NC_000913.3.
DR RefSeq; WP_000949502.1; NZ_LN832404.1.
DR AlphaFoldDB; P39305; -.
DR SMR; P39305; -.
DR BioGRID; 4262715; 7.
DR IntAct; P39305; 1.
DR STRING; 511145.b4197; -.
DR PaxDb; P39305; -.
DR PRIDE; P39305; -.
DR EnsemblBacteria; AAC77154; AAC77154; b4197.
DR EnsemblBacteria; BAE78198; BAE78198; BAE78198.
DR GeneID; 948712; -.
DR KEGG; ecj:JW4155; -.
DR KEGG; eco:b4197; -.
DR PATRIC; fig|1411691.4.peg.2504; -.
DR EchoBASE; EB2390; -.
DR eggNOG; COG3623; Bacteria.
DR HOGENOM; CLU_082738_0_0_6; -.
DR InParanoid; P39305; -.
DR OMA; QAGMGHI; -.
DR PhylomeDB; P39305; -.
DR BioCyc; EcoCyc:G7859-MON; -.
DR BioCyc; MetaCyc:G7859-MON; -.
DR UniPathway; UPA00263; UER00379.
DR PRO; PR:P39305; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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; IDA:EcoCyc.
DR GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; IEP:EcoCyc.
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 2: Evidence at transcript level;
KW Isomerase; Reference proteome.
FT CHAIN 1..284
FT /note="L-ribulose-5-phosphate 3-epimerase UlaE"
FT /id="PRO_0000097716"
SQ SEQUENCE 284 AA; 32007 MW; AAA9F000B9D94A08 CRC64;
MLSKQIPLGI YEKALPAGEC WLERLQLAKT LGFDFVEMSV DETDDRLSRL NWSREQRLAL
VNAIVETGVR VPSMCLSAHR RFPLGSEDDA VRAQGLEIMR KAIQFAQDVG IRVIQLAGYD
VYYQEANNET RRRFRDGLKE SVEMASRAQV TLAMEIMDYP LMSSISKALG YAHYLNNPWF
QLYPDIGNLS AWDNDVQMEL QAGIGHIVAV HVKDTKPGVF KNVPFGEGVV DFERCFETLK
QSGYCGPYLI EMWSETAEDP AAEVAKARDW VKARMAKAGM VEAA
