[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/s002849900392; PubMed=9767718 [NCBI, ExPASy, EBI, Israel, Japan] Clark M.A., Baumann L., Baumann P.; "Buchnera aphidicola (Aphid endosymbiont) contains genes encoding enzymes of histidine biosynthesis."; Curr. Microbiol. 37:356-358(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan] Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; "50 million years of genomic stasis in endosymbiotic bacteria."; Science 296:2376-2379(2002).

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

AF067228; AAC97355.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE013218; AAM67663.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_660452.1; -.

3D structure databases

HSSP

P06988; 1KAE. [HSSP ENTRY / PDB]

ModBase

Q9ZHE6.

Enzyme and pathway databases

BioCyc

BAPH198804:BUSG093-MON; -.

Ontologies

GO:0004399;	Molecular function: histidinol dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0000105;	Biological process: histidine biosynthetic process (inferred from electronic annotation from HAMAP).
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]

TIGRFAMs

TIGR00069; hisD; 1.

PROSITE

PS00611; HISOL_DEHYDROGENASE; 1.

BLOCKS

Q9ZHE6.

Genome annotation databases

GeneID

1005910; -.

GenomeReviews

AE013218_GR; BUsg_093.

KEGG

bas:BUsg093; -.

Phylogenomic databases

HOGENOM

Q9ZHE6; -.

Genome annotation databases

CMR

Q9ZHE6; BUsg_093.

Other

ProtoNet

Q9ZHE6.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 435`	`435`	`Histidinol dehydrogenase.`	`PRO_0000135746`
`ACT_SITE`	`327 327`		`Proton acceptor (By similarity).`
`ACT_SITE`	`328 328`		`Proton acceptor (By similarity).`
`METAL`	`260 260`		`Zinc (By similarity).`
`METAL`	`263 263`		`Zinc (By similarity).`
`METAL`	`361 361`		`Zinc (By similarity).`
`METAL`	`420 420`		`Zinc (By similarity).`
`BINDING`	`131 131`		`NAD (By similarity).`
`BINDING`	`189 189`		`NAD (By similarity).`
`BINDING`	`212 212`		`NAD (By similarity).`
`BINDING`	`238 238`		`Substrate (By similarity).`
`BINDING`	`260 260`		`Substrate (By similarity).`
`BINDING`	`263 263`		`Substrate (By similarity).`
`BINDING`	`328 328`		`Substrate (By similarity).`
`BINDING`	`361 361`		`Substrate (By similarity).`
`BINDING`	`415 415`		`Substrate (By similarity).`
`BINDING`	`420 420`		`Substrate (By similarity).`

Sequence information

Length: 435 AA [This is the length of the unprocessed precursor]

Molecular weight: 47738 Da [This is the MW of the unprocessed precursor]

CRC64: CD25387C2B62BDE2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKYFNTIVNW NMLNSNEQKN ILLRPVIKNN NSIKKKVKKI IENIQVLGEK ALREYTILFE 

        70         80         90        100        110        120 
KCHINKFEVS KEKMLSSSLY VNQSLKDAIS TAKKNITSFH TAQILSPIDI ETQVGVRCQQ 

       130        140        150        160        170        180 
IYLPLNSVGI YIPSGIAPLF STVLMLAIPA KIAGCKQIIL CSPPPIDNTI LYAANICGVD 

       190        200        210        220        230        240 
KIFQMGGAQA IAALAFGTKN IPKVDKIFGP GNAYVTEAKL QVSSIFNGPQ IDMLAGPSEL 

       250        260        270        280        290        300 
LIIADEASNA DFIAADLLSQ AEHSISSQVI LLTPSLQLAK KVIISINNQL KNLSKSDDIS 

       310        320        330        340        350        360 
TALDNSVIIL TKDLFECIKI SNIYAPEHLI IQTKEPRLIL KEILNASSIF LGPWSPESAG 

       370        380        390        400        410        420 
DYASGTNHVL PTYGKSVSSS ALGLCDFKKR VLIQELTSQG FINLSNTLKI LSEAEKLEAH 

       430 
KNAVKIRVDF LKEKI

Q9ZHE6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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