ULAD_SHIF8
ID ULAD_SHIF8 Reviewed; 216 AA.
AC Q0SX89;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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}; OrderedLocusNames=SFV_4352;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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; CP000266; ABF06326.1; -; Genomic_DNA.
DR RefSeq; WP_000056760.1; NC_008258.1.
DR AlphaFoldDB; Q0SX89; -.
DR SMR; Q0SX89; -.
DR EnsemblBacteria; ABF06326; ABF06326; SFV_4352.
DR GeneID; 66671891; -.
DR KEGG; sfv:SFV_4352; -.
DR HOGENOM; CLU_081825_0_0_6; -.
DR OMA; WEQAQEW; -.
DR BioCyc; SFLE373384:SFV_RS23950-MON; -.
DR UniPathway; UPA00263; UER00378.
DR Proteomes; UP000000659; 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_1000067321"
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
