ID   ULAF_ECOLC              Reviewed;         228 AA.
AC   B1IT08;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   16-JUN-2009, entry version 8.
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=EcolC_3815;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000946; ACA79419.1; -; Genomic_DNA.
DR   RefSeq; YP_001726746.1; -.
DR   GeneID; 6064755; -.
DR   GenomeReviews; CP000946_GR; EcolC_3815.
DR   KEGG; ecl:EcolC_3815; -.
DR   OMA; B1IT08; DAEPLHT.
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_1000088485.
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;  25280 MW;  06D867A89F9E6B4A CRC64;
     MQKLKQQVFE ANMELPRYGL ATFTWGNVSA IDRERGLVVI KPSGVAYETM KAADMVVVDM
     SGKVVEGEYR PSSDTATHLE LYRRYPSLGG IVHTHSTHAT AWAQAGLAIP ALGTTHADYF
     FGDIPCTRGL SEEEVQGEYE LNTGKVIIET LGNAEPLHTP GIVVYQHGPF AWGKDAHDAV
     HNAVVMEEVA KMAWIARSIN PQLNHIDSFL MNKHFMRKHG PNAYYGQK
//