NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Vergez L., Larimer F., Land M., Lykidis A., Richardson P.;
"Complete sequence of a megaplasmid of Ralstonia eutropha JMP134.";
Submitted (AUG-2005) 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

CP000092; AAZ65418.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_293275.1; -.

3D structure databases

ModBase

Q46N53.

Enzyme and pathway databases

BioCyc

REUT264198:REUT_C6092-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

3607398; -.

GenomeReviews

CP000092_GR; Reut_C6092.

KEGG

reu:Reut_C6092; -.

NMPDR

fig|264198.3.peg.6; -.

Phylogenomic databases

HOGENOM

Q46N53; -.

Genome annotation databases

CMR

Q46N53; Reut_C6092.

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; Plasmid; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 436`	`436`	`Histidinol dehydrogenase 2.`	`PRO_0000135827`
`ACT_SITE`	`318 318`		`Proton acceptor (By similarity).`
`ACT_SITE`	`319 319`		`Proton acceptor (By similarity).`
`METAL`	`248 248`		`Zinc (By similarity).`
`METAL`	`251 251`		`Zinc (By similarity).`
`METAL`	`352 352`		`Zinc (By similarity).`
`METAL`	`411 411`		`Zinc (By similarity).`
`BINDING`	`118 118`		`NAD (By similarity).`
`BINDING`	`180 180`		`NAD (By similarity).`
`BINDING`	`203 203`		`NAD (By similarity).`
`BINDING`	`226 226`		`Substrate (By similarity).`
`BINDING`	`248 248`		`Substrate (By similarity).`
`BINDING`	`251 251`		`Substrate (By similarity).`
`BINDING`	`319 319`		`Substrate (By similarity).`
`BINDING`	`352 352`		`Substrate (By similarity).`
`BINDING`	`406 406`		`Substrate (By similarity).`
`BINDING`	`411 411`		`Substrate (By similarity).`

Sequence information

Length: 436 AA [This is the length of the unprocessed precursor]

Molecular weight: 46881 Da [This is the MW of the unprocessed precursor]

CRC64: E505337929A7046C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MISYLKKAEK TPQTETATAQ KVVTEMLAEI QARGKDAVRQ YAKQLDGWSG DIVLTPDQIR 

        70         80         90        100        110        120 
EQTKDVPAGV RADIDFAIRQ VTDFALAQRE SLKEFSVELH PGVTAGQRVL PVNVVGCYAP 

       130        140        150        160        170        180 
AGRYAHIASA YMGVATAKAA GVKTVVACSS PFRGQGIHPH VLYAFQAAGA DVIMALGGVQ 

       190        200        210        220        230        240 
AIASMAYGLF TGKPADVVVG PGNKFVAEAK RSLYGQVGID VFAGPSEVAV IADETADPAI 

       250        260        270        280        290        300 
VASDLVGQAE HGHESPAWLF TTSRDLADRV MALVPELIAK LPPTARDAAT AAWRDYGEVI 

       310        320        330        340        350        360 
LCGTREEVVE ISDRYASEHL EVHTADLDWW LANLTCYGSL FLGEETTVAF GDKTSGPNHV 

       370        380        390        400        410        420 
LPTKGAARYS GGLSVHKFMK TLTWQQMTRE ATRQIGQVTA RISRLEGMEA HARTADDRMA 

       430 
KYFPNASFEM GTPVEV

Q46N53 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