ID   ULAF_ECOL5              Reviewed;         228 AA.
AC   Q0T9J5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=ECP_4443;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(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; CP000247; ABG72384.1; -; Genomic_DNA.
DR   RefSeq; YP_672285.1; -.
DR   GeneID; 4190035; -.
DR   GenomeReviews; CP000247_GR; ECP_4443.
DR   KEGG; ecp:ECP_4443; -.
DR   NMPDR; fig|340197.3.peg.946; -.
DR   HOGENOM; Q0T9J5; -.
DR   OMA; Q0T9J5; DAEPLHT.
DR   BioCyc; ECOL362663:ECP_4443-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_1000070639.
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;  25306 MW;  C2C942553FF3B464 CRC64;
     MQKLKQQVFE ANMDLPHYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM KADDMVVVDM
     SGNVVEGEYR PSSDTATHLE LYRRYPSLGG IVHTHSTHAT AWAQAGLAIP ALGTTHADYF
     FGDIPCTRGL SEEEVQGEYE LNTGKVIIET LGDAEPLHTP GIVVYQHGPF AWGKDAHDAV
     HNAVVMEEVA KMAWIARSIN PQLNHIDSFL MNKHFMRKHG PNAYYGQK
//