ID W1F240_ECOLX Unreviewed; 216 AA.
AC W1F240;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=3-keto-L-gulonate-6-phosphate decarboxylase UlaD {ECO:0000256|HAMAP-Rule:MF_01267};
DE EC=4.1.1.85 {ECO:0000256|HAMAP-Rule:MF_01267};
DE AltName: Full=3-dehydro-L-gulonate-6-phosphate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01267};
DE AltName: Full=KGPDC {ECO:0000256|HAMAP-Rule:MF_01267};
DE AltName: Full=L-ascorbate utilization protein D {ECO:0000256|HAMAP-Rule:MF_01267};
GN Name=ulaD {ECO:0000256|HAMAP-Rule:MF_01267};
OS Escherichia coli ISC7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=1432555 {ECO:0000313|EMBL:CDL27082.1, ECO:0000313|Proteomes:UP000019199};
RN [1] {ECO:0000313|EMBL:CDL27082.1, ECO:0000313|Proteomes:UP000019199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISC7 {ECO:0000313|EMBL:CDL27082.1,
RC ECO:0000313|Proteomes:UP000019199};
RA Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., Wiesinger-Mayr H.;
RT "Antibiotic resistance diversity of beta-lactamase producers in the General
RT Hospital Vienna.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01267};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01267};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01267};
CC -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose 5-
CC phosphate from L-ascorbate: step 2/4. {ECO:0000256|HAMAP-
CC Rule:MF_01267}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01267}.
CC -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR.
CC {ECO:0000256|HAMAP-Rule:MF_01267}.
CC -!- SIMILARITY: Belongs to the HPS/KGPDC family. KGPDC subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01267}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDL27082.1}.
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; CBWN010000076; CDL27082.1; -; Genomic_DNA.
DR AlphaFoldDB; W1F240; -.
DR SMR; W1F240; -.
DR UniPathway; UPA00263; UER00378.
DR Proteomes; UP000019199; Unassembled WGS sequence.
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; Aldolase class I; 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 PANTHER; PTHR35039; 3-KETO-L-GULONATE-6-PHOSPHATE DECARBOXYLASE SGBH-RELATED; 1.
DR PANTHER; PTHR35039:SF3; 3-KETO-L-GULONATE-6-PHOSPHATE DECARBOXYLASE SGBH-RELATED; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01267};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_01267};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01267};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01267};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01267}.
FT DOMAIN 5..207
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01267"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01267"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01267"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01267"
FT SITE 64
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01267"
FT SITE 67
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01267"
SQ SEQUENCE 216 AA; 23578 MW; EC8490DA1D02D824 CRC64;
MSLPMLQVAL DNQTMDSAYE TTRLIAEEVD IIEVGTILCV GEGVRAVRDL KALYPHKIVL
ADAKIADAGK ILSRMCFEAN ADWVTVICCA DINTAKGALD VAKEFNGDVQ IELTGYWTWE
QAQQWRDAGI GQVVYHRSRD AQAAGVAWGE ADITAIKRLS DMGFKVTVTG GLALEDLPLF
KGIPIHVFIA GRSIRDAASP VEAARQFKRS IAELWG
//
