[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1128/JB.185.11.3333-3343.2003; PubMed=12754231 [NCBI, ExPASy, EBI, Israel, Japan] Komatsu H., Imura Y., Ohori A., Nagata Y., Tsuda M.; "Distribution and organization of auxotrophic genes on the multichromosomal genome of Burkholderia multivorans ATCC 17616."; J. Bacteriol. 185:3333-3343(2003).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.; "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC 17616."; Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E., Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N., Hattori M., Tsuda M.; "Complete genome sequence of Burkholderia multivorans ATCC 17616."; Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.

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 .
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

AB091436; BAC65270.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000868; ABX14023.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009385; BAG44811.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001578520.1; -.
YP_001947347.1; -.

3D structure databases

ModBase

Q845V3.

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.
IPR002035; VWF_A.
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.
PR00453; VWFADOMAIN.

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

Q845V3.

Genome annotation databases

GeneID

5765433; -.
6359505; -.

CMR

Q845V3; Bmul_0328.

Other

ProtoNet

Q845V3.

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`	`1 438`	`438`	`Histidinol dehydrogenase.`	`PRO_0000135749`
`ACT_SITE`	`335 335`		`Proton acceptor (By similarity).`
`ACT_SITE`	`336 336`		`Proton acceptor (By similarity).`
`METAL`	`267 267`		`Zinc (By similarity).`
`METAL`	`270 270`		`Zinc (By similarity).`
`METAL`	`369 369`		`Zinc (By similarity).`
`METAL`	`428 428`		`Zinc (By similarity).`
`BINDING`	`138 138`		`NAD (By similarity).`
`BINDING`	`199 199`		`NAD (By similarity).`
`BINDING`	`222 222`		`NAD (By similarity).`
`BINDING`	`245 245`		`Substrate (By similarity).`
`BINDING`	`267 267`		`Substrate (By similarity).`
`BINDING`	`270 270`		`Substrate (By similarity).`
`BINDING`	`336 336`		`Substrate (By similarity).`
`BINDING`	`369 369`		`Substrate (By similarity).`
`BINDING`	`423 423`		`Substrate (By similarity).`
`BINDING`	`428 428`		`Substrate (By similarity).`
`CONFLICT`	`90 101`		`AALEAAAARVRG -> GRAGSGCRTRAR (in Ref. 1; BAC65270).`

Sequence information

Length: 438 AA [This is the length of the unprocessed precursor]

Molecular weight: 46515 Da [This is the MW of the unprocessed precursor]

CRC64: 8F702C8C7E014B1D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSITIRKLDS TSEGFDAALR AVLAFEASED EAIERSVAQI LADVKSRGDA AVLEYTNRFD 

        70         80         90        100        110        120 
RLNADSVAAL ELPQDALQAA LDGLEPKARA ALEAAAARVR GYHEKQKIEC GTHSWQYTES 

       130        140        150        160        170        180 
DGTVLGQKIT PLDRVGLYVP GGKAAYPSSV LMNAIPARVA GVGEIVMVVP TPDGVKNDLV 

       190        200        210        220        230        240 
LAAALLGGVD RVFTIGGAQA VGALAYGTAT VPAVDKICGP GNAYVASAKR RVFGTVGIDM 

       250        260        270        280        290        300 
IAGPSEILVL CDGTTDPSWV AMDLFSQAEH DELAQSILLC PDASFIERVE KAIAELLPSM 

       310        320        330        340        350        360 
PRQDVIRASL EGRGALIKVR DMTEACRIAN DIAPEHLEIS ALEPQQWSQQ IRHAGAIFLG 

       370        380        390        400        410        420 
RYTSESLGDY CAGPNHVLPT SRTARFSSPL GVYDFIKRSS LIEVSAEGAH TLGEIAAELA 

       430 
YGEGLQAHAK SAEFRMKG

Q845V3 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