NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=YCH46;
DOI=10.1073/pnas.0404172101; PubMed=15466707 [NCBI, ExPASy, EBI, Israel, Japan]
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation.";
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).

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

AP006841; BAD49934.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_100468.1; -.

3D structure databases

ModBase

Q64RE7.

Enzyme and pathway databases

BioCyc

BFRA295405:BF3189-MON; -.

Ontologies

GO:0004399;	Molecular function: histidinol dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
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.

ProtoNet

Q64RE7.

Genome annotation databases

3083091; -.

AP006841_GR; BF3189.

bfr:BF3189; -.

fig|295405.3.peg.3530; -.

Phylogenomic databases

HOGENOM

Q64RE7; -.

Genome annotation databases

CMR

Q64RE7; BF3189.

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`	`1 428`	`428`	`Histidinol dehydrogenase.`	`PRO_0000135730`
`ACT_SITE`	`322 322`		`Proton acceptor (By similarity).`
`ACT_SITE`	`323 323`		`Proton acceptor (By similarity).`
`METAL`	`255 255`		`Zinc (By similarity).`
`METAL`	`258 258`		`Zinc (By similarity).`
`METAL`	`356 356`		`Zinc (By similarity).`
`METAL`	`415 415`		`Zinc (By similarity).`
`BINDING`	`124 124`		`NAD (By similarity).`
`BINDING`	`186 186`		`NAD (By similarity).`
`BINDING`	`209 209`		`NAD (By similarity).`
`BINDING`	`233 233`		`Substrate (By similarity).`
`BINDING`	`255 255`		`Substrate (By similarity).`
`BINDING`	`258 258`		`Substrate (By similarity).`
`BINDING`	`323 323`		`Substrate (By similarity).`
`BINDING`	`356 356`		`Substrate (By similarity).`
`BINDING`	`410 410`		`Substrate (By similarity).`
`BINDING`	`415 415`		`Substrate (By similarity).`

Sequence information

Length: 428 AA [This is the length of the unprocessed precursor]

Molecular weight: 46530 Da [This is the MW of the unprocessed precursor]

CRC64: BDFEB76D7C6BEB2A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKLIKYPDRS QWNEILKRPV LETENLFDTV RNIINRVRAG GDRVVMECEA VFDKAELTSL 

        70         80         90        100        110        120 
AVTSAEIEEA EKEVPIELKA AIYLAKRNIE TFHSAQRFEG KKVDTMEGVT CWQKAVAIEK 

       130        140        150        160        170        180 
VGLYIPGGTA PLFSTVLMLA IPAKIAGCKE IVLCTPPDKN GKVHPAILFA ARLAGVSKIF 

       190        200        210        220        230        240 
KVGGVQAIAA MAYGTESIPK VYKIFGPGNQ YVTAAKQLVS LRDVAIDMPA GPSEVEVLAD 

       250        260        270        280        290        300 
ESANPVFVAA DLLSQAEHGV DSQAMLVTTS EKLQTEVVYE VERQLGYLTR RDIAEKSLAN 

       310        320        330        340        350        360 
SKLILVKDME EALELTNAYA PEHLIIETKD YMEVAGQIVN AGSVFLGAFS PESAGDYASG 

       370        380        390        400        410        420 
TNHTLPTNGY AKAYSGVSLD SFIRKITFQE ILPSGMSAIG PAIEVMAANE HLDAHKNAVT 


VRLEEIRK

Q64RE7 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