ULAE_SHISS
ID ULAE_SHISS Reviewed; 284 AA.
AC Q3YUF1;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=SSON_4379;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ90861.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3YUF1; -.
DR SMR; Q3YUF1; -.
DR EnsemblBacteria; AAZ90861; AAZ90861; SSON_4379.
DR KEGG; ssn:SSON_4379; -.
DR HOGENOM; CLU_082738_0_0_6; -.
DR OMA; QAGMGHI; -.
DR UniPathway; UPA00263; UER00379.
DR Proteomes; UP000002529; 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_0000233260"
SQ SEQUENCE 284 AA; 32075 MW; 16D6E726374732ED CRC64;
MLSKQIPLGI YEKALPAGEC WLERLRLAKT LGFDFVEMSV DETDERLSRL DWSREQRLAL
VNAIVETGVR VPSMCLSAHR RFPLGSEDDA VRAQGLEIMR KAIQFAQDVG IRVIQLAGYD
VYYQEANNET RRRFRDGLKE SVEMASRAQV TLAMEIMDYP LMNSISKALG YAHYLNNPWF
QLYPDIGNLS AWDNDVQMEL QAGIGHIVAV HVKDTKPGVF KNVPFGEGVV DFERCFETLK
QSGYCGPYLI EMWSETAEDP AAEVVKARDW VKARMAKAGT VEAA