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   16-JUN-2009, entry version 31.
DE   RecName: Full=L-ribulose-5-phosphate 3-epimerase ulaE;
DE            EC=5.1.3.22;
DE   AltName: Full=L-xylulose-5-phosphate 3-epimerase;
DE   AltName: Full=L-ascorbate utilization protein E;
GN   Name=ulaE; OrderedLocusNames=SSON_4379;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Catalyzes the isomerization of L-xylulose-5-phosphate to
CC       L-ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate
CC       utilization (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-ribulose 5-phosphate = L-xylulose 5-
CC       phosphate.
CC   -!- PATHWAY: Cofactor degradation; L-ascorbic acid degradation; D-
CC       xylulose 5-phosphate from L-ascorbic acid: step 3/4.
CC   -!- INDUCTION: Induced by L-ascorbate. Repressed by ulaR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the HUMPI family.
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DR   EMBL; CP000038; AAZ90861.1; -; Genomic_DNA.
DR   RefSeq; YP_313096.1; -.
DR   GeneID; 3668421; -.
DR   GenomeReviews; CP000038_GR; SSON_4379.
DR   KEGG; ssn:SSON_4379; -.
DR   HOGENOM; Q3YUF1; -.
DR   OMA; Q3YUF1; VVKARDW.
DR   BioCyc; SSON300269:SSO_4379-MON; -.
DR   GO; GO:0016861; F:intramolecular oxidoreductase activity, int...; IEA:InterPro.
DR   GO; GO:0034015; F:L-ribulose-5-phosphate 3-epimerase activity; IEA:HAMAP.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0019852; P:L-ascorbic acid metabolic process; IEA:HAMAP.
DR   HAMAP; MF_01951; -; 1.
DR   InterPro; IPR004560; Hxl6Piso_put.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   InterPro; IPR012307; Xyl_isomerase-typ_TIM-brl.
DR   Gene3D; G3DSA:3.20.20.150; Xyl_isomerase-like_TIM-brl; 1.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   TIGRFAMs; TIGR00542; hxl6Piso_put; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Isomerase.
FT   CHAIN         1    284       L-ribulose-5-phosphate 3-epimerase ulaE.
FT                                /FTId=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
//