ULAE_SALTY
ID ULAE_SALTY Reviewed; 284 AA.
AC Q8ZK86;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=STM4387;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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; AE006468; AAL23207.1; -; Genomic_DNA.
DR RefSeq; NP_463248.1; NC_003197.2.
DR RefSeq; WP_000949525.1; NC_003197.2.
DR AlphaFoldDB; Q8ZK86; -.
DR SMR; Q8ZK86; -.
DR STRING; 99287.STM4387; -.
DR PaxDb; Q8ZK86; -.
DR EnsemblBacteria; AAL23207; AAL23207; STM4387.
DR GeneID; 1255913; -.
DR KEGG; stm:STM4387; -.
DR PATRIC; fig|99287.12.peg.4612; -.
DR HOGENOM; CLU_082738_0_0_6; -.
DR OMA; QAGMGHI; -.
DR PhylomeDB; Q8ZK86; -.
DR BioCyc; SENT99287:STM4387-MON; -.
DR UniPathway; UPA00263; UER00379.
DR Proteomes; UP000001014; 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; IBA:GO_Central.
DR GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..284
FT /note="L-ribulose-5-phosphate 3-epimerase UlaE"
FT /id="PRO_0000233256"
SQ SEQUENCE 284 AA; 31820 MW; 7D12E8B816D03391 CRC64;
MLSKQIPLGI YEKALPAGEC WLERLRLAKT LGFDFVEMSV DETDARLARL DWSREQRLAL
VSAVAETGVR VPSMCLSAHR RFPLGSEDDA IRAQGLEIMR KAIQFAQDVG IRVIQLAGYD
VYYQQANDET RCRFRDGLKE SVDMASRAQV TLAMEIMDYP LMNSISKALG YAHYLNNPWF
QLYPDIGNLS AWDNDVQMEL QAGIGHIVAV HVKDTKPGVF KNVPFGEGVV DFERCFETLK
QSGYCGPYLI EMWSETAENP AAEVAKARDW VKARMASAGL VEAA