ULAF_SALTY
ID ULAF_SALTY Reviewed; 228 AA.
AC Q8ZK85;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
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}; OrderedLocusNames=STM4388;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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; AE006468; AAL23208.1; -; Genomic_DNA.
DR RefSeq; NP_463249.1; NC_003197.2.
DR RefSeq; WP_001170771.1; NC_003197.2.
DR AlphaFoldDB; Q8ZK85; -.
DR SMR; Q8ZK85; -.
DR STRING; 99287.STM4388; -.
DR PaxDb; Q8ZK85; -.
DR EnsemblBacteria; AAL23208; AAL23208; STM4388.
DR GeneID; 1255914; -.
DR KEGG; stm:STM4388; -.
DR PATRIC; fig|99287.12.peg.4613; -.
DR HOGENOM; CLU_006033_5_0_6; -.
DR OMA; SWLMNKH; -.
DR PhylomeDB; Q8ZK85; -.
DR BioCyc; SENT99287:STM4388-MON; -.
DR UniPathway; UPA00263; UER00380.
DR Proteomes; UP000001014; 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; 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 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 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_0000233247"
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; 25327 MW; 16399B00A84E55A8 CRC64;
MQKLKQQVFD ANMDLPRYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM KVDDMVVVDM
DGKVVEGRYR PSSDTATHLA LYQRYPSLGG VVHTHSTHAT AWAQAGMAIP ALGTTHADYF
FGDIPCTRAL SEEEVQGEYE LNTGKVIIET LGEVEPLHTP GIVVYQHGPF AWGKDAHDAV
HNAVVMEEVA RMAWIARGIN PALNPIDDYL MNKHFMRKHG PNAYYGQK
