ID   ULAE_SHIF8              Reviewed;         284 AA.
AC   Q0SX88;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=SFV_4353;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z.,
RA   Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y.,
RA   Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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; CP000266; ABF06327.1; -; Genomic_DNA.
DR   RefSeq; YP_691632.1; -.
DR   GeneID; 4208608; -.
DR   GenomeReviews; CP000266_GR; SFV_4353.
DR   KEGG; sfv:SFV_4353; -.
DR   HOGENOM; Q0SX88; -.
DR   OMA; Q0SX88; VVKARDW.
DR   BioCyc; SFLE373384:SFV_4353-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_1000070635.
SQ   SEQUENCE   284 AA;  32079 MW;  4138EA24F37E0ACE CRC64;
     MLSKQIPLGI YEKALPAGEC WLERLRLAKT LGFDFVEMSV DETNERLSRL DWSRVQRLAL
     VNAIVETGVR VPSMCLSAHR RFPLVSEDDA VRAQGLEIMR KAIQFAQDVG IRVIQLSGYD
     VYYQEANNET RRRFRDGLKE SVEMASRAQV TLAMEIMDYP LMNSISKALG YAHYLNNPWF
     QLYPDIGNLS AWDNDVQMEL QAGIGHIVAV HVKDTKPGVF KNVPFGEGVV DFERCFETLK
     QSGYCGPYLI EMWSETAEDP AAEVVKACDW VKARMAKAGM VEAA
//