ID   ULAF_SHIF8              Reviewed;         228 AA.
AC   Q0SX87;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=L-ribulose-5-phosphate 4-epimerase ulaF;
DE            EC=5.1.3.4;
DE   AltName: Full=Phosphoribulose isomerase;
DE   AltName: Full=L-ascorbate utilization protein F;
GN   Name=ulaF; OrderedLocusNames=SFV_4354;
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-ribulose 5-phosphate to
CC       D-xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate
CC       utilization (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-ribulose 5-phosphate = D-xylulose 5-
CC       phosphate.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (Potential).
CC   -!- PATHWAY: Cofactor degradation; L-ascorbic acid degradation; D-
CC       xylulose 5-phosphate from L-ascorbic acid: step 4/4.
CC   -!- INDUCTION: Induced by L-ascorbate. Repressed by ulaR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the aldolase class II family. AraD/fucA
CC       subfamily.
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DR   EMBL; CP000266; ABF06328.1; -; Genomic_DNA.
DR   RefSeq; YP_691633.1; -.
DR   GeneID; 4208609; -.
DR   GenomeReviews; CP000266_GR; SFV_4354.
DR   KEGG; sfv:SFV_4354; -.
DR   HOGENOM; Q0SX87; -.
DR   OMA; Q0SX87; DAEPLHT.
DR   BioCyc; SFLE373384:SFV_4354-MON; -.
DR   GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019852; P:L-ascorbic acid metabolic process; IEA:HAMAP.
DR   HAMAP; MF_01952; -; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   Gene3D; G3DSA:3.40.225.10; Aldolase_II/adducin_N; 1.
DR   Pfam; PF00596; Aldolase_II; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Isomerase; Metal-binding; Zinc.
FT   CHAIN         1    228       L-ribulose-5-phosphate 4-epimerase ulaF.
FT                                /FTId=PRO_1000070640.
FT   METAL        74     74       Zinc (By similarity).
FT   METAL        93     93       Zinc (By similarity).
FT   METAL        95     95       Zinc (By similarity).
FT   METAL       167    167       Zinc (By similarity).
SQ   SEQUENCE   228 AA;  25354 MW;  A9F842E53CD8EE98 CRC64;
     MQKLKQQVFE ANMDLPRYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM KADDMVVVDM
     SGKVVEGEYR PSSDTATHLE LYRRYPSLGG IVHTHSTHAT AWAQAGLAIP ALGTTHADYF
     FGDIPCTRGL SEEEVQGEYE LNTGKVIIET LGNAEPLHTP GIVVYQHGPF AWGKDAHDAV
     HNAVVMEEVA KMAWIARSIN PQLNHIDSYL MNKHFMRKHG PNAYYGQK
//