ID   ULAF_SHIBS              Reviewed;         228 AA.
AC   P0C1B9;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   14-APR-2009, entry version 20.
DE   RecName: Full=Putative 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=SBO_4257;
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268;
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-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.
CC   -!- CAUTION: Could be the product of a pseudogene.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CP000036; Type=Erroneous termination; Positions=172; Note=Translated as Trp;
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DR   EMBL; CP000036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   GenomeReviews; CP000036_GR; SBO_4257.
DR   KEGG; sbo:SBO_4257; -.
DR   HOGENOM; P0C1B9; -.
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   5: Uncertain;
KW   Complete proteome; Isomerase; Metal-binding; Zinc.
FT   CHAIN         1    228       Putative L-ribulose-5-phosphate 4-
FT                                epimerase ulaF.
FT                                /FTId=PRO_0000234033.
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;  25338 MW;  978176AF708AEE90 CRC64;
     MQKLKQQVFE ANMDLPRYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM KADDMVVVDM
     SGKVVEGKYR PSSDTATHLE LYRRYPSLGG IVHTHSTHAT AWAQAGLAIP ALGTTHADYF
     FGDIPCTRGL SEEEVQGEYE LNTGKVIIET LGDAEPLHTP GIVVYQHGPF AWGKDAHDAV
     HNAVVMEEVA KMAWIARSIN PQLNHIDSFL MNKHFMRKHG PNAYYGQK
//