AC   MF_01825;
DC   Protein; auto
TR   HAMAP; MF_01825; -; 1; level=0
XX
Names: PdxB
XX
ID   PDXB
DE   RecName: Full=Erythronate-4-phosphate dehydrogenase;
DE            EC=1.1.1.290;
GN   Name=pdxB;
XX
CC   -!- FUNCTION: Catalyzes the oxidation of erythronate-4-phosphate to 3-
CC       hydroxy-2-oxo-4-phosphonooxybutanoate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-
CC         phosphooxybutanoate + H(+) + NADH; Xref=Rhea:RHEA:18829,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58538, ChEBI:CHEBI:58766; EC=1.1.1.290;
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC       pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. PdxB subfamily.
XX
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1; trigger=no
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1; trigger=no
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1; trigger=no
DR   Pfam; PF00389; 2-Hacid_dh; 1; trigger=no
DR   Pfam; PF02826; 2-Hacid_dh_C; 1; trigger=no
DR   PRINTS; PR00411; PNDRDTASEI; 1; trigger=no
XX
KW   Cytoplasm
KW   NAD
KW   Oxidoreductase
KW   Pyridoxine biosynthesis
XX
GO   GO:0016491; F:oxidoreductase activity
GO   GO:0008615; P:pyridoxine biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: PDXB_PSEAE (Q9I3W9)
FT   BINDING         126..127
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Optional; Condition: Q-V
FT   BINDING         206..208
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Optional; Condition: A-S-R
FT   ACT_SITE        208
FT   Condition: R
FT   ACT_SITE        237
FT   Condition: E
FT   ACT_SITE        254
FT                   /note="Proton donor"
FT   Condition: H
FT   BINDING         45
FT                   /ligand="substrate"
FT   Optional; Condition: [ST]
FT   BINDING         66
FT                   /ligand="substrate"
FT   Optional; Condition: T
FT   BINDING         146
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Optional; Condition: D
FT   BINDING         175
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Optional; Condition: T
FT   BINDING         232
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Optional; Condition: D
FT   BINDING         257
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Optional; Condition: G
FT   BINDING         258
FT                   /ligand="substrate"
FT   Optional; Condition: Y
XX
Size: 345-393;
Related: None;
Template: P05459; Q9I3W9;
Scope:
 Bacteria; Bacteroidota
 Bacteria; Gammaproteobacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: The pyridoxal phosphate can be synthetised from two separate branches: the
 pdxA branch (that requires the gapA (or epd), pdxB, serC and pdxA enzymes)
 and the pdxJ branch (that requires the dxs and pdxJ enzymes) that start
 different precursors. Both branches for the last step (pdxH) of the
 from pyridoxal phosphate pathway.
XX
# Revision 1.19 2022/11/19
//