ULAF_ECOLI
ID ULAF_ECOLI Reviewed; 228 AA.
AC P39306; Q2M6A7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=L-ribulose-5-phosphate 4-epimerase UlaF {ECO:0000255|HAMAP-Rule:MF_01952, ECO:0000303|PubMed:11741871};
DE EC=5.1.3.4 {ECO:0000255|HAMAP-Rule:MF_01952, ECO:0000269|PubMed:11741871};
DE AltName: Full=L-ascorbate utilization protein F {ECO:0000255|HAMAP-Rule:MF_01952, ECO:0000303|PubMed:11741871};
DE AltName: Full=Phosphoribulose isomerase {ECO:0000255|HAMAP-Rule:MF_01952};
GN Name=ulaF {ECO:0000255|HAMAP-Rule:MF_01952, ECO:0000303|PubMed:11741871};
GN Synonyms=sgaE, yjfX; OrderedLocusNames=b4198, JW4156;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP DISCUSSION OF SEQUENCE.
RA Reizer J., Charbit A., Reizer A., Saier M.H. Jr.;
RT "Novel phosphotransferases system genes revealed by bacterial genome
RT analysis: operons encoding homologues of sugar-specific permease domains of
RT the phosphotransferase system and pentose catabolic enzymes.";
RL Genome Sci. Technol. 1:53-75(1996).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11741871; DOI=10.1128/jb.184.1.302-306.2002;
RA Yew W.S., Gerlt J.A.;
RT "Utilization of L-ascorbate by Escherichia coli K-12: assignments of
RT functions to products of the yjf-sga and yia-sgb operons.";
RL J. Bacteriol. 184:302-306(2002).
RN [6]
RP INDUCTION.
RX PubMed=12374842; DOI=10.1128/jb.184.21.6065-6068.2002;
RA Campos E., Aguilar J., Baldoma L., Badia J.;
RT "The gene yjfQ encodes the repressor of the yjfR-X regulon (ula), which is
RT involved in L-ascorbate metabolism in Escherichia coli.";
RL J. Bacteriol. 184:6065-6068(2002).
RN [7]
RP INDUCTION.
RX PubMed=14996803; DOI=10.1128/jb.186.6.1720-1728.2004;
RA Campos E., Baldoma L., Aguilar J., Badia J.;
RT "Regulation of expression of the divergent ulaG and ulaABCDEF operons
RT involved in L-ascorbate dissimilation in Escherichia coli.";
RL J. Bacteriol. 186:1720-1728(2004).
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 ECO:0000269|PubMed:11741871}.
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 ECO:0000269|PubMed:11741871};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P08203,
CC ECO:0000255|HAMAP-Rule:MF_01952};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08203,
CC ECO:0000255|HAMAP-Rule:MF_01952};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=657 uM for L-ribulose 5-phosphate (LRu5P)
CC {ECO:0000269|PubMed:11741871};
CC Note=kcat is 25 sec(-1) with L-ribulose 5-phosphate (LRu5P) as
CC substrate. {ECO:0000269|PubMed:11741871};
CC -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose 5-
CC phosphate from L-ascorbate: step 4/4. {ECO:0000255|HAMAP-Rule:MF_01952,
CC ECO:0000269|PubMed:11741871}.
CC -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR.
CC {ECO:0000255|HAMAP-Rule:MF_01952, ECO:0000269|PubMed:12374842,
CC ECO:0000269|PubMed:14996803}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01952}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U14003; AAA97094.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77155.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78199.1; -; Genomic_DNA.
DR PIR; S56423; S56423.
DR RefSeq; NP_418619.1; NC_000913.3.
DR RefSeq; WP_001170847.1; NZ_LN832404.1.
DR AlphaFoldDB; P39306; -.
DR SMR; P39306; -.
DR BioGRID; 4262716; 6.
DR DIP; DIP-10868N; -.
DR IntAct; P39306; 12.
DR STRING; 511145.b4198; -.
DR PaxDb; P39306; -.
DR PRIDE; P39306; -.
DR EnsemblBacteria; AAC77155; AAC77155; b4198.
DR EnsemblBacteria; BAE78199; BAE78199; BAE78199.
DR GeneID; 948711; -.
DR KEGG; ecj:JW4156; -.
DR KEGG; eco:b4198; -.
DR PATRIC; fig|1411691.4.peg.2503; -.
DR EchoBASE; EB2391; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_006033_5_0_6; -.
DR InParanoid; P39306; -.
DR OMA; SWLMNKH; -.
DR PhylomeDB; P39306; -.
DR BioCyc; EcoCyc:G7860-MON; -.
DR BioCyc; MetaCyc:G7860-MON; -.
DR UniPathway; UPA00263; UER00380.
DR PRO; PR:P39306; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central.
DR GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; IEP:EcoCyc.
DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
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_0000162921"
FT ACT_SITE 118
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P08203, ECO:0000255|HAMAP-
FT Rule:MF_01952"
FT ACT_SITE 225
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P08203, ECO:0000255|HAMAP-
FT Rule:MF_01952"
FT BINDING 26..27
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB87, ECO:0000255|HAMAP-
FT Rule:MF_01952"
FT BINDING 43..44
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB87, ECO:0000255|HAMAP-
FT Rule:MF_01952"
FT BINDING 72..73
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB87, ECO:0000255|HAMAP-
FT Rule:MF_01952"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P08203, ECO:0000255|HAMAP-
FT Rule:MF_01952"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P08203, ECO:0000255|HAMAP-
FT Rule:MF_01952"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P08203, ECO:0000255|HAMAP-
FT Rule:MF_01952"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P08203, ECO:0000255|HAMAP-
FT 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