NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2034659 [NCBI, ExPASy, EBI, Israel, Japan]
Nagai A., Ward E., Beck J., Tada S., Chang J.-Y., Scheidegger A., Ryals J.;
"Structural and functional conservation of histidinol dehydrogenase between plants and microbes.";
Proc. Natl. Acad. Sci. U.S.A. 88:4133-4137(1991).

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 .
SUBCELLULAR LOCATION: Plastid, chloroplast.
MISCELLANEOUS: Cabbage may contain multiple HDH isozymes encoded by different genes.
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

M60466; AAA32991.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A39358; A39358.

3D structure databases

HSSP

P06988; 1K75. [HSSP ENTRY / PDB]

ModBase

P24226.

Family and domain databases

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.

Other

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

Keywords

Amino-acid biosynthesis; Chloroplast; Direct protein sequencing; Histidine biosynthesis; Metal-binding; NAD; Oxidoreductase; Plastid; Transit peptide; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 31`	`31`	`Chloroplast.`
`CHAIN`	`32 469`	`438`	`Histidinol dehydrogenase, chloroplastic.`	`PRO_0000007216`
`ACT_SITE`	`357 357`		`Proton acceptor (By similarity).`
`ACT_SITE`	`358 358`		`Proton acceptor (By similarity).`
`METAL`	`289 289`		`Zinc (By similarity).`
`METAL`	`292 292`		`Zinc (By similarity).`
`METAL`	`391 391`		`Zinc (By similarity).`
`METAL`	`450 450`		`Zinc (By similarity).`
`BINDING`	`156 156`		`NAD (By similarity).`
`BINDING`	`218 218`		`NAD (By similarity).`
`BINDING`	`241 241`		`NAD (By similarity).`
`BINDING`	`267 267`		`Substrate (By similarity).`
`BINDING`	`289 289`		`Substrate (By similarity).`
`BINDING`	`292 292`		`Substrate (By similarity).`
`BINDING`	`358 358`		`Substrate (By similarity).`
`BINDING`	`391 391`		`Substrate (By similarity).`
`BINDING`	`445 445`		`Substrate (By similarity).`
`BINDING`	`450 450`		`Substrate (By similarity).`

Sequence information

Length: 469 AA [This is the length of the unprocessed precursor]

Molecular weight: 50959 Da [This is the MW of the unprocessed precursor]

CRC64: EC63FA4B7B2E19CA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSFDLSRLSL TSSPRLSFLT RTATKKGFVR CSMKSYRLSE LSFSQVENLK ARPRIDFSSI 

        70         80         90        100        110        120 
FTTVNPIIDA VRSKGDTAVK EYTERFDKVQ LNKVVEDVSE LDIPELDSAV KEAFDVAYDN 

       130        140        150        160        170        180 
IYAFHFAQMS TEKSVENMKG VRCKRVSRSI GSVGLYVPGG TAVLPSTALM LAIPAQIAGC 

       190        200        210        220        230        240 
KTVVLATPPT KEGSICKEVL YCAKRAGVTH ILKAGGAQAI AAMAWGTDSC PKVEKIFGPG 

       250        260        270        280        290        300 
NQYVTAAKMI LQNSEAMVSI DMPAGPSEVL VIADEHASPV YIAADLLSQA EHGPDSQVVL 

       310        320        330        340        350        360 
VVVGDGVNLK AIEEEIAKQC KSLPRGEFAS KALSHSFTVF ARDMIEAITF SNLYAPEHLI 

       370        380        390        400        410        420 
INVKDAEKWE GLIENAGSVF IGPWTPESVG DYASGTNHVL PTYGYARMYS GVSLDSFLKF 

       430        440        450        460 
MTVQSLTEEG LRNLGPYVAT MAEIEGLDAH KRAVTLRLKD IEAKQTQTK

P24226 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