AC   MF_01024;
DC   Protein; auto
TR   HAMAP; MF_01024; -; 1; level=0
XX
Names: HisD
XX
ID   HISX
DE   RecName: Full=Histidinol dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.23;
GN   Name=hisD;
XX
CC   -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC       histidinol to L-histidinaldehyde and then to L-histidine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH;
CC         Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699,
CC         ChEBI:CHEBI:57945; EC=1.1.1.23;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
end case
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
case <OC:Enterobacterales>
CC   -!- SUBUNIT: Homodimer.
end case
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
XX
DR   Pfam; PF00815; Histidinol_dh; 1; trigger=no
DR   PRINTS; PR00083; HOLDHDRGNASE; 1; trigger=no
DR   NCBIfam; TIGR00069; HisD; 1; trigger=no
DR   PROSITE; PS00611; HISOL_DEHYDROGENASE; 1; trigger=no
XX
KW   Amino-acid biosynthesis
KW   Histidine biosynthesis
KW   Oxidoreductase
KW   NAD
case <FTGroup:1>
KW   Metal-binding
KW   Zinc
end case
XX
GO   GO:0004399; F:histidinol dehydrogenase activity
case <FTGroup:1>
GO   GO:0008270; F:zinc ion binding
end case
GO   GO:0000105; P:histidine biosynthetic process
XX
FT   From: HISX_ECOLI (P06988)
FT   ACT_SITE        326
FT                   /note="Proton acceptor"
FT   Condition: E
FT   ACT_SITE        327
FT                   /note="Proton acceptor"
FT   Condition: H
FT   BINDING         259
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: [EQ]
FT   BINDING         262
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         360
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: D
FT   BINDING         419
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         130
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Group: 2; Condition: Y
FT   BINDING         188
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Group: 2; Condition: Q
FT   BINDING         211
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Group: 2; Condition: N
FT   BINDING         237
FT                   /ligand="substrate"
FT   Group: 3; Condition: [ST]
FT   BINDING         259
FT                   /ligand="substrate"
FT   Group: 3; Condition: Q
FT   BINDING         262
FT                   /ligand="substrate"
FT   Group: 3; Condition: H
FT   BINDING         327
FT                   /ligand="substrate"
FT   Group: 3; Condition: H
FT   BINDING         360
FT                   /ligand="substrate"
FT   Group: 3; Condition: D
FT   BINDING         414
FT                   /ligand="substrate"
FT   Group: 3; Condition: E
FT   BINDING         419
FT                   /ligand="substrate"
FT   Group: 3; Condition: H
XX
Size: 368-480;
Related: None;
Template: P06988; P10370;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: MF_01023 (hisC)
Duplicate: in NOSS1, TRIV2
Plasmid: in RHIME
Comments: PHOLL is a fusion between hisC and hisD. As other Enterobacterales
 do not have such a fusion, this could be a sequencing artefact.
XX
# Revision 1.38 2023/06/01
//