NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(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 .
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

BA000040; BAC46521.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_767896.1; -.

3D structure databases

HSSP

P06988; 1K75. [HSSP ENTRY / PDB]

ModBase

P59397.

Enzyme and pathway databases

BioCyc

BJAP224911:BLR1256-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).
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]

TIGRFAMs

TIGR00069; hisD; 1.

PROSITE

PS00611; HISOL_DEHYDROGENASE; 1.

Genome annotation databases

GeneID

1049433; -.

GenomeReviews

BA000040_GR; blr1256.

KEGG

bja:blr1256; -.

NMPDR

fig|224911.1.peg.1256; -.

Phylogenomic databases

HOGENOM

P59397; -.

Genome annotation databases

CMR

P59397; blr1256.

Other

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`	`1 431`	`431`	`Histidinol dehydrogenase.`	`PRO_0000135739`
`ACT_SITE`	`327 327`		`Proton acceptor (By similarity).`
`ACT_SITE`	`328 328`		`Proton acceptor (By similarity).`
`METAL`	`259 259`		`Zinc (By similarity).`
`METAL`	`262 262`		`Zinc (By similarity).`
`METAL`	`361 361`		`Zinc (By similarity).`
`METAL`	`420 420`		`Zinc (By similarity).`
`BINDING`	`130 130`		`NAD (By similarity).`
`BINDING`	`191 191`		`NAD (By similarity).`
`BINDING`	`214 214`		`NAD (By similarity).`
`BINDING`	`237 237`		`Substrate (By similarity).`
`BINDING`	`259 259`		`Substrate (By similarity).`
`BINDING`	`262 262`		`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: 431 AA [This is the length of the unprocessed precursor]

Molecular weight: 44907 Da [This is the MW of the unprocessed precursor]

CRC64: 6FBB4505AD936B6D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPVRLDRSSA DFDQRFAAFL AAKREVSADV EAAARAIVDD VARRGDAALL EATAKFDRLT 

        70         80         90        100        110        120 
LDASGLRVSA AEIEAAVKAC DAATLDALSL ARDRIETYHR RQLPKDERFT DPLGVELGWR 

       130        140        150        160        170        180 
YTAIESAGLY VPGGTAAYPS SVLMNAVPAK VAGVSRLVMV VPSPDGKLNP LVLAAARLGG 

       190        200        210        220        230        240 
VTEIYRVGGA QAVAALAHGT ATIAPVAKIV GPGNAYVAAA KRLVFGKVGI DMIAGPSEVL 

       250        260        270        280        290        300 
VIADDTGNAD WIAADLLAQA EHDTSAQSIL ITDSARLAAD VEKAVEAQLK TLPRTAIASA 

       310        320        330        340        350        360 
SWADFGAIIM VKNLNDAIPL ADAIAAEHLE IMTTDPDALA ARIRNAGAVF LGAHTPEAIG 

       370        380        390        400        410        420 
DYVGGSNHVL PTARSARFSS GLSVHDFMKR TSILKCGPDQ LRALGPAAMT LGKAEGLDAH 

       430 
SRSIGLRLNL S

P59397 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