ULAF_ECO57
ID ULAF_ECO57 Reviewed; 228 AA.
AC Q8XDI4; Q7A8U5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=Z5807, ECs5174;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG59394.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38597.1; -; Genomic_DNA.
DR PIR; F86116; F86116.
DR PIR; F91275; F91275.
DR RefSeq; NP_313201.1; NC_002695.1.
DR RefSeq; WP_001170812.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XDI4; -.
DR SMR; Q8XDI4; -.
DR STRING; 155864.EDL933_5543; -.
DR EnsemblBacteria; AAG59394; AAG59394; Z5807.
DR EnsemblBacteria; BAB38597; BAB38597; ECs_5174.
DR GeneID; 913993; -.
DR KEGG; ece:Z5807; -.
DR KEGG; ecs:ECs_5174; -.
DR PATRIC; fig|386585.9.peg.5408; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_006033_5_0_6; -.
DR OMA; SWLMNKH; -.
DR UniPathway; UPA00263; UER00380.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome;
KW Zinc.
FT CHAIN 1..228
FT /note="L-ribulose-5-phosphate 4-epimerase UlaF"
FT /id="PRO_0000233242"
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; 25338 MW; A9F842F35008EE98 CRC64;
MQKLKQQVFE ANMDLPRYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM KADDMVVVDM
SGKVVEGEYR PSSDTATHLE LYRRYPSLGG IVHTHSTHAT AWAQAGLAIP ALGTTHADYF
FGDIPCTRGL SEEEVQGEYE LNTGKVIIET LGNAEPLHTP GIVVYQHGPF AWGKDAHDAV
HNAVVMEEVA KMAWIARSIN PQLNHIDSFL MNKHFMRKHG PNAYYGQK
