[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=10555290 [NCBI, ExPASy, EBI, Israel, Japan] Clark M.A., Moran N.A., Baumann P.; "Sequence evolution in bacterial endosymbionts having extreme base compositions."; Mol. Biol. Evol. 16:1586-1598(1999).

Comments

FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine (By similarity).
CATALYTIC ACTIVITY: L-histidinol + 2 NAD⁺ = L-histidine + 2 NADH.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9 .
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the histidinol dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF129282; AAF13773.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P06988; 1K75. [HSSP ENTRY / PDB]

ModBase

Q9RQ85.

Ontologies

GO:0004399;	Molecular function: histidinol dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0000105;	Biological process: histidine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01024; -; 1.
PBIL [Tree]

InterPro

IPR001692; Histidinol_DHase.
IPR012131; Hstdl_DHase_prok.
Graphical view of domain structure.

PANTHER

PTHR21256:SF2; Hstdl_DH_prok; 1.

Pfam

PF00815; Histidinol_dh; 1.
Pfam graphical view of domain structure.

PRINTS

PR00083; HOLDHDRGNASE.

ProDom

PD002680; Histidinol_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00611; HISOL_DEHYDROGENASE; PARTIAL.

ProtoNet

Q9RQ85.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Histidine biosynthesis; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 >201`	`>201`	`Histidinol dehydrogenase.`	`PRO_0000135747`
`NON_TER`	`201 201`

Sequence information

Length: 201 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 22668 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 9C0370E1A3894358 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHNILEVIYW NKCSYERKKK ILSRPIISNR FLIRNKVKEI ISNVKSFGDR ALYNYTNVFD 

        70         80         90        100        110        120 
NINLKNIRVS EEDIVSSHLH VSKELKLAVE VAFKNIKKFH SKQNVGSFNL KVQDNIYCQQ 

       130        140        150        160        170        180 
IIRPIESIGL YIPNGSAPLL STVLMLAIPA NIAGCKRIML CSPPPIMNEI LYACKICEIK 

       190        200 
DVFQIGGAQA IAALGCGTET I

Q9RQ85 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools