HAMAP rule MF_01024
General rule information
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| Accession | MF_01024 |
| Dates | 20-MAR-2003 (Created)
1-JUN-2023 (Last updated, Version 38) |
| Name | HisD |
| Scope(s) |
Bacteria Archaea |
| Template(s) | P06988 (HISX_ECOLI); P10370 (HISX_SALTY); [ Recover all ] |
| Triggered by |
HAMAP; MF_01024 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | HISX |
| Protein name | RecName: Full=Histidinol dehydrogenase; Short=HDH; EC=1.1.1.23; |
| Gene name | Name=hisD; |
Comments
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| FUNCTION | Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. |
| CATALYTIC ACTIVITY | Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; |
| case <FTGroup:1> | |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; |
| end case | |
| PATHWAY | Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. |
| case <OC:Enterobacterales> | |
| SUBUNIT | Homodimer. |
| end case | |
| SIMILARITY | Belongs to the histidinol dehydrogenase family. |
Keywords
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| Amino-acid biosynthesis | |
| Histidine biosynthesis | |
| Oxidoreductase | |
| NAD | |
| case <FTGroup:1> | |
| Metal-binding | |
| Zinc | |
| end case | |
Gene Ontology
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| GO:0004399; Molecular function:histidinol dehydrogenase activity | |
| case <FTGroup:1> | |
| GO:0008270; Molecular function:zinc ion binding | |
| end case | |
| GO:0000105; Biological process:histidine biosynthetic process | |
Cross-references
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| Pfam | PF00815; Histidinol_dh; 1; |
| PRINTS | PR00083; HOLDHDRGNASE; 1; |
| NCBIfam | TIGR00069; HisD; 1; |
| PROSITE | PS00611; HISOL_DEHYDROGENASE; 1; |
Features
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| From: HISX_ECOLI (P06988) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 326 | 326 | /note="Proton acceptor" | E | ||||||||
| ACT_SITE | 327 | 327 | /note="Proton acceptor" | H | ||||||||
| BINDING | 259 | 259 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
[EQ] | 1 | |||||||
| BINDING | 262 | 262 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 1 | |||||||
| BINDING | 360 | 360 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
D | 1 | |||||||
| BINDING | 419 | 419 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 1 | |||||||
| BINDING | 130 | 130 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
Y | 2 | |||||||
| BINDING | 188 | 188 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
Q | 2 | |||||||
| BINDING | 211 | 211 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
N | 2 | |||||||
| BINDING | 237 | 237 | /ligand="substrate" | [ST] | 3 | |||||||
| BINDING | 259 | 259 | /ligand="substrate" | Q | 3 | |||||||
| BINDING | 262 | 262 | /ligand="substrate" | H | 3 | |||||||
| BINDING | 327 | 327 | /ligand="substrate" | H | 3 | |||||||
| BINDING | 360 | 360 | /ligand="substrate" | D | 3 | |||||||
| BINDING | 414 | 414 | /ligand="substrate" | E | 3 | |||||||
| BINDING | 419 | 419 | /ligand="substrate" | H | 3 | |||||||
Additional information
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| Size range | 368-480 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: MF_01023 (hisC) |
| Comments | PHOLL is a fusion between hisC and hisD. As other Enterobacterales do not have such a fusion, this could be a sequencing artefact. |