ULAD_ECO24
ID ULAD_ECO24 Reviewed; 216 AA.
AC A7ZV66;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=3-keto-L-gulonate-6-phosphate decarboxylase UlaD {ECO:0000255|HAMAP-Rule:MF_01267};
DE EC=4.1.1.85 {ECO:0000255|HAMAP-Rule:MF_01267};
DE AltName: Full=3-dehydro-L-gulonate-6-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01267};
DE AltName: Full=KGPDC {ECO:0000255|HAMAP-Rule:MF_01267};
DE AltName: Full=L-ascorbate utilization protein D {ECO:0000255|HAMAP-Rule:MF_01267};
GN Name=ulaD {ECO:0000255|HAMAP-Rule:MF_01267};
GN OrderedLocusNames=EcE24377A_4757;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
CC -!- FUNCTION: Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into
CC L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization.
CC {ECO:0000255|HAMAP-Rule:MF_01267}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-L-gulonate 6-phosphate + H(+) = CO2 + L-xylulose 5-
CC phosphate; Xref=Rhea:RHEA:14353, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57829, ChEBI:CHEBI:58774; EC=4.1.1.85;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01267};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01267};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01267};
CC -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose 5-
CC phosphate from L-ascorbate: step 2/4. {ECO:0000255|HAMAP-
CC Rule:MF_01267}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01267}.
CC -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR.
CC {ECO:0000255|HAMAP-Rule:MF_01267}.
CC -!- SIMILARITY: Belongs to the HPS/KGPDC family. KGPDC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01267}.
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DR EMBL; CP000800; ABV17772.1; -; Genomic_DNA.
DR RefSeq; WP_000056760.1; NC_009801.1.
DR AlphaFoldDB; A7ZV66; -.
DR SMR; A7ZV66; -.
DR EnsemblBacteria; ABV17772; ABV17772; EcE24377A_4757.
DR GeneID; 66671891; -.
DR KEGG; ecw:EcE24377A_4757; -.
DR HOGENOM; CLU_081825_0_0_6; -.
DR OMA; WEQAQEW; -.
DR UniPathway; UPA00263; UER00378.
DR Proteomes; UP000001122; Chromosome.
DR GO; GO:0033982; F:3-dehydro-L-gulonate-6-phosphate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd04726; KGPDC_HPS; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01267; UlaD; 1.
DR InterPro; IPR023942; 3-keto-L-gulonate6Pdecase_UlaD.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR041710; HPS/KGPDC.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Decarboxylase; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..216
FT /note="3-keto-L-gulonate-6-phosphate decarboxylase UlaD"
FT /id="PRO_1000067318"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01267"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01267"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01267"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01267"
FT SITE 64
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01267"
FT SITE 67
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01267"
SQ SEQUENCE 216 AA; 23649 MW; CDF287AC1D1BAD68 CRC64;
MSLPMLQVAL DNQTMDSAYE TTRLIAEEVD IIEVGTILCV GEGVRAVRDL KALYPHKIVL
ADAKIADAGK ILSRMCFEAN ADWVTVICCA DINTAKGALD VAKEFNGDVQ IELTGYWTWE
QAQQWRDAGI QQVVYHRSRD AQAAGVAWGE ADITAIKRLS DMGFKVTVTG GLALEDLPLF
KGIPIHVFIA GRSIRDAASP VEAARQFKRS IAELWG
