ULAE_ECO57
ID ULAE_ECO57 Reviewed; 284 AA.
AC Q8XDI5; Q7A8U6;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
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};
GN OrderedLocusNames=Z5806, ECs5173;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG59393.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38596.1; -; Genomic_DNA.
DR PIR; E86116; E86116.
DR PIR; E91275; E91275.
DR RefSeq; NP_313200.1; NC_002695.1.
DR RefSeq; WP_000949511.1; NZ_SWKA01000005.1.
DR PDB; 3CQH; X-ray; 2.08 A; A/B=2-284.
DR PDB; 3CQI; X-ray; 2.10 A; A/B=2-284.
DR PDB; 3CQJ; X-ray; 2.04 A; A/B=2-284.
DR PDB; 3CQK; X-ray; 2.33 A; A/B=2-284.
DR PDBsum; 3CQH; -.
DR PDBsum; 3CQI; -.
DR PDBsum; 3CQJ; -.
DR PDBsum; 3CQK; -.
DR AlphaFoldDB; Q8XDI5; -.
DR SMR; Q8XDI5; -.
DR STRING; 155864.EDL933_5542; -.
DR EnsemblBacteria; AAG59393; AAG59393; Z5806.
DR EnsemblBacteria; BAB38596; BAB38596; ECs_5173.
DR GeneID; 913998; -.
DR KEGG; ece:Z5806; -.
DR KEGG; ecs:ECs_5173; -.
DR PATRIC; fig|386585.9.peg.5407; -.
DR eggNOG; COG3623; Bacteria.
DR HOGENOM; CLU_082738_0_0_6; -.
DR OMA; QAGMGHI; -.
DR UniPathway; UPA00263; UER00379.
DR EvolutionaryTrace; Q8XDI5; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..284
FT /note="L-ribulose-5-phosphate 3-epimerase UlaE"
FT /id="PRO_0000233251"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:3CQJ"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3CQJ"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:3CQJ"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:3CQJ"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:3CQJ"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:3CQJ"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:3CQJ"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:3CQJ"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:3CQJ"
FT HELIX 89..109
FT /evidence="ECO:0007829|PDB:3CQJ"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:3CQJ"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3CQJ"
FT HELIX 128..148
FT /evidence="ECO:0007829|PDB:3CQJ"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:3CQJ"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3CQJ"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:3CQJ"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:3CQJ"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:3CQJ"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:3CQJ"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:3CQJ"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3CQJ"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3CQJ"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:3CQJ"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:3CQJ"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:3CQJ"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:3CQJ"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:3CQJ"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:3CQJ"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:3CQH"
FT HELIX 260..277
FT /evidence="ECO:0007829|PDB:3CQJ"
SQ SEQUENCE 284 AA; 32049 MW; 16D6E783072733F2 CRC64;
MLSKQIPLGI YEKALPAGEC WLERLQLAKT LGFDFVEMSV DETDERLSRL DWSREQRLAL
VNAIVETGVR VPSMCLSAHR RFPLGSEDDA VRAQGLEIMR KAIQFAQDVG IRVIQLAGYD
VYYQEANNET RRRFRDGLKE SVEMASRAQV TLAMEIMDYP LMNSISKALG YAHYLNNPWF
QLYPDIGNLS AWDNDVQMEL QAGIGHIVAV HVKDTKPGVF KNVPFGEGVV DFERCFETLK
QSGYCGPYLI EMWSETAEDP AAEVAKARDW VKARMAKAGM VEAA
