ID   ULAD_SHIB3              Reviewed;         216 AA.
AC   B2TY68;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=SbBS512_E4726;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) 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: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; CP001063; ACD07252.1; -; Genomic_DNA.
DR   RefSeq; WP_000056766.1; NC_010658.1.
DR   AlphaFoldDB; B2TY68; -.
DR   SMR; B2TY68; -.
DR   STRING; 344609.SbBS512_E4726; -.
DR   EnsemblBacteria; ACD07252; ACD07252; SbBS512_E4726.
DR   KEGG; sbc:SbBS512_E4726; -.
DR   HOGENOM; CLU_081825_0_0_6; -.
DR   OMA; WEQAQEW; -.
DR   UniPathway; UPA00263; UER00378.
DR   Proteomes; UP000001030; 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_1000140126"
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;  23677 MW;  CDF287BFBF919668 CRC64;
     MSLPMLQVAL DNQTMDSAYE TTRLIAEEVD IIEVGTILCV GEGVRAVRDL KALYPHKIVL
     ADAKIADAGK ILSRMCFEAN ADWVTVICCA DINTAKGALD VAKEFNGDVQ IELTGYWTWE
     QAQQWRDAGI QQVVYHRSRD AQAAGVAWGE ADITAIKRLS DMGFKVTVTG GLVLEDLPLF
     KGIPIHVFIA GRSIRDAASP VEAARQFKRS IAELWG