ULAF_ECO7I
ID ULAF_ECO7I Reviewed; 228 AA.
AC B7NTQ4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=L-ribulose-5-phosphate 4-epimerase UlaF {ECO:0000255|HAMAP-Rule:MF_01952};
DE EC=5.1.3.4 {ECO:0000255|HAMAP-Rule:MF_01952};
DE AltName: Full=L-ascorbate utilization protein F {ECO:0000255|HAMAP-Rule:MF_01952};
DE AltName: Full=Phosphoribulose isomerase {ECO:0000255|HAMAP-Rule:MF_01952};
GN Name=ulaF {ECO:0000255|HAMAP-Rule:MF_01952};
GN OrderedLocusNames=ECIAI39_4663;
OS Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI39 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Catalyzes the isomerization of L-ribulose 5-phosphate to D-
CC xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate
CC utilization. {ECO:0000255|HAMAP-Rule:MF_01952}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ribulose 5-phosphate = D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:22368, ChEBI:CHEBI:57737, ChEBI:CHEBI:58226;
CC EC=5.1.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_01952};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01952};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01952};
CC -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose 5-
CC phosphate from L-ascorbate: step 4/4. {ECO:0000255|HAMAP-
CC Rule:MF_01952}.
CC -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR.
CC {ECO:0000255|HAMAP-Rule:MF_01952}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01952}.
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DR EMBL; CU928164; CAR20761.1; -; Genomic_DNA.
DR RefSeq; WP_001170785.1; NC_011750.1.
DR RefSeq; YP_002410524.1; NC_011750.1.
DR AlphaFoldDB; B7NTQ4; -.
DR SMR; B7NTQ4; -.
DR STRING; 585057.ECIAI39_4663; -.
DR EnsemblBacteria; CAR20761; CAR20761; ECIAI39_4663.
DR KEGG; ect:ECIAI39_4663; -.
DR PATRIC; fig|585057.6.peg.4810; -.
DR HOGENOM; CLU_006033_5_0_6; -.
DR OMA; SWLMNKH; -.
DR UniPathway; UPA00263; UER00380.
DR Proteomes; UP000000749; Chromosome.
DR GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.225.10; -; 1.
DR HAMAP; MF_01952; UlaF; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR023499; UlaF.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Isomerase; Metal-binding; Zinc.
FT CHAIN 1..228
FT /note="L-ribulose-5-phosphate 4-epimerase UlaF"
FT /id="PRO_1000188843"
FT ACT_SITE 118
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01952"
FT ACT_SITE 225
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01952"
FT BINDING 26..27
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01952"
FT BINDING 43..44
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01952"
FT BINDING 72..73
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01952"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01952"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01952"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01952"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01952"
SQ SEQUENCE 228 AA; 25310 MW; BC40C2793E6C7E73 CRC64;
MQKLKQQVFE ANMDLPRYGL VTFTWGNVSA IDRERGLVVI KPSGIAYESM KAADMVVVDM
SGKVVEGEYR PSSDTATHLE LYRRYPSLGG IVHTHSTHAT AWAQAGLAIP ALGTTHADYF
FGDIPCTRGL SEEEVQGEYE LNTGKVIIET LGNAEPLHTP GIVVYQHGPF AWGKDAHDAV
HNAVVMEEVA KMAWIARSIN PQLNHIDSYL MNKHFMRKHG PNAYYGQK
