ID   ULAD_ECODH              Reviewed;         216 AA.
AC   B1XDU7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=ECDH10B_4391;
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 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; CP000948; ACB05184.1; -; Genomic_DNA.
DR   RefSeq; WP_000056749.1; NC_010473.1.
DR   AlphaFoldDB; B1XDU7; -.
DR   SMR; B1XDU7; -.
DR   GeneID; 67414814; -.
DR   KEGG; ecd:ECDH10B_4391; -.
DR   HOGENOM; CLU_081825_0_0_6; -.
DR   OMA; WEQAQEW; -.
DR   BioCyc; ECOL316385:ECDH10B_RS22400-MON; -.
DR   UniPathway; UPA00263; UER00378.
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_1000140113"
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;  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