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ULAE_SALPB
ID   ULAE_SALPB              Reviewed;         284 AA.
AC   A9N513;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=SPAB_05521;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000886; ABX70790.1; -; Genomic_DNA.
DR   RefSeq; WP_000949530.1; NC_010102.1.
DR   AlphaFoldDB; A9N513; -.
DR   SMR; A9N513; -.
DR   KEGG; spq:SPAB_05521; -.
DR   PATRIC; fig|1016998.12.peg.5174; -.
DR   HOGENOM; CLU_082738_0_0_6; -.
DR   OMA; QAGMGHI; -.
DR   BioCyc; SENT1016998:SPAB_RS22545-MON; -.
DR   UniPathway; UPA00263; UER00379.
DR   Proteomes; UP000008556; 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_1000088484"
SQ   SEQUENCE   284 AA;  31806 MW;  65BBC9223D791201 CRC64;
     MLSKQIPLGI YEKALPAGEC WLERLRLAKT LGFDFVEMSV DETDARLARL DWSREQRLAL
     VSAVAETGVR VPSMCLSAHR RFPLGSEDDA VRAQGLEIMR KAIQFAQDVG IRVIQLAGYD
     VYYQQANDET RCRFRDGLKE SVDMASRAQV TLAMEIMDYP LMNSISKALG YAHYLNNPWF
     QLYPDIGNLS AWDNDVQMEL QAGIGHIVAV HVKDTKPGVF KNVPFGEGVV DFERCFETLK
     QSGYCGPYLI EMWSETAENP AAEVAKARDW VKARMASAGL VEAA
 
 
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