AC   MF_01267;
DC   Protein; auto
TR   HAMAP; MF_01267; -; 1; level=0
XX
Names: UlaD
XX
ID   ULAD
DE   RecName: Full=3-keto-L-gulonate-6-phosphate decarboxylase UlaD;
DE            EC=4.1.1.85;
DE   AltName: Full=3-dehydro-L-gulonate-6-phosphate decarboxylase;
DE   AltName: Full=KGPDC;
DE   AltName: Full=L-ascorbate utilization protein D;
GN   Name=ulaD;
XX
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   -!- 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;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
end case
CC   -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose 5-
CC       phosphate from L-ascorbate: step 2/4.
CC   -!- SUBUNIT: Homodimer.
CC   -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR.
CC   -!- SIMILARITY: Belongs to the HPS/KGPDC family. KGPDC subfamily.
XX
DR   Pfam; PF00215; OMPdecase; 1; trigger=no
XX
KW   Carbohydrate metabolism
KW   Decarboxylase
KW   Lyase
case <FTGroup:1>
KW   Magnesium
KW   Metal-binding
end case
XX
case <FTGroup:1>
GO   GO:0000287; F:magnesium ion binding
end case
GO   GO:0016831; F:carboxy-lyase activity
GO   GO:0019854; P:L-ascorbic acid catabolic process
XX
FT   From: ULAD_ECOLI (P39304)
FT   BINDING         33
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: E
FT   BINDING         62
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         11
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         192
FT                   /ligand="substrate"
FT   Condition: R
FT   SITE            64
FT                   /note="Transition state stabilizer"
FT   SITE            67
FT                   /note="Transition state stabilizer"
XX
Size: 216-216;
Related: None;
Template: P39304;
Scope:
 Bacteria; Enterobacterales
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.20 2022/11/19
//