ULAF_ECODH
ID ULAF_ECODH Reviewed; 228 AA.
AC B1XDU9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=ECDH10B_4393;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
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; CP000948; ACB05186.1; -; Genomic_DNA.
DR RefSeq; WP_001170847.1; NC_010473.1.
DR AlphaFoldDB; B1XDU9; -.
DR SMR; B1XDU9; -.
DR KEGG; ecd:ECDH10B_4393; -.
DR HOGENOM; CLU_006033_5_0_6; -.
DR OMA; SWLMNKH; -.
DR BioCyc; ECOL316385:ECDH10B_RS22410-MON; -.
DR UniPathway; UPA00263; UER00380.
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_1000188846"
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; 25278 MW; 3E96E7E0261E36B6 CRC64;
MQKLKQQVFE ANMELPRYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM KAADMVVVDM
SGKVVEGEYR PSSDTATHLE LYRRYPSLGG IVHTHSTHAT AWAQAGLAIP ALGTTHADYF
FGDIPCTRGL SEEEVQGEYE LNTGKVIIET LGNAEPLHTP GIVVYQHGPF AWGKDAHDAV
HNAVVMEEVA KMAWIARGIN PQLNHIDSFL MNKHFMRKHG PNAYYGQK
