Reviewed, UniProtKB/Swiss-Prot Q7VSZ1 (HISX_BORPE)

Names and origin

Protein names

Recommended name:
    Histidinol dehydrogenase
      Short name=HDH
    EC=1.1.1.23

Gene names

Name:	hisD
Ordered Locus Names:	BP3768

Organism

Bordetella pertussis [Complete proteome] [HAMAP]

Taxonomic identifier

520 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity. HAMAP MF_01024
Catalytic activity	L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_01024
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP MF_01024
Sequence similarities	Belongs to the histidinol dehydrogenase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 434	434	Histidinol dehydrogenase HAMAP MF_01024		PRO_0000135738
Sites
	Active site	330	1	Proton acceptor By similarity
	Active site	331	1	Proton acceptor By similarity
	Metal binding	262	1	Zinc By similarity
	Metal binding	265	1	Zinc By similarity
	Metal binding	364	1	Zinc By similarity
	Metal binding	423	1	Zinc By similarity
	Binding site	133	1	NAD By similarity
	Binding site	194	1	NAD By similarity
	Binding site	217	1	NAD By similarity
	Binding site	240	1	Substrate By similarity
	Binding site	262	1	Substrate By similarity
	Binding site	265	1	Substrate By similarity
	Binding site	331	1	Substrate By similarity
	Binding site	364	1	Substrate By similarity
	Binding site	418	1	Substrate By similarity
	Binding site	423	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7VSZ1-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: D2D494FB6AE5EB6A	FASTA	434	46,136
	10 20 30 40 50 60 MALINRLDSR DPGFKTALSQ LLAFEAEQDE SIDQAAAGIL ADVRRRGDAA LLEYTQRFDR 70 80 90 100 110 120 LAVDDATALE IPQADWHAAL DSLPAAQRQA LEAAAARVRA YHERQRGETW TYTEADGTML 130 140 150 160 170 180 GQQITALDRV GLYVPGGKAA YPSSVLMNAI PAKVAGVPEL IMVTPTPDGV RNPIVLAAAA 190 200 210 220 230 240 IAGVDRAFAI GGAQAVGALA YGTATVPAVD KIVGPGNAYV AAAKRRVFGT VGIDMIAGPS 250 260 270 280 290 300 EILVICDGKT PADWIAMDLF SQAEHDELAQ SILLCPDAAF LAEVEAAIER LLPGMPRADI 310 320 330 340 350 360 LRVSLANRGA LILVRDLEEA CAIANDIAPE HLEISTEQPQ RWTALIRHAG AIFMGRYSSE 370 380 390 400 410 420 ALGDYCAGPN HVLPTSRTAR FSSPLGVYDF QKRSSLIQVS REGAQTLGRI AAELALGEGL 430 QAHAASAQYR LDQP

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tohama I / ATCC BAA-589 / NCTC 13251.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640422 Genomic DNA. Translation: CAE44024.1.
RefSeq	NP_882269.1.
3D structure databases
SMR	Q7VSZ1. Positions 26-433.
ModBase	Search...
Genome annotation databases
GeneID	2665051.
KEGG	bpe:BP3768.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG329596.
OMA	LDAHKNA.
PhylomeDB	Q7VSZ1.
Enzyme and pathway databases
BioCyc	BPER257313:BP3768-MONOMER.
BRENDA	1.1.1.23. 21511.
Family and domain databases
HAMAP	MF_01024. HisD. [Tree]
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR001692. Histidinol_DH_CS. IPR012131. Hstdl_DH_prok-type. [Graphical view]
PANTHER	PTHR21256:SF2. Hstdl_DH_prok. 1 hit.
Pfam	PF00815. Histidinol_dh. 1 hit. [Graphical view]
PRINTS	PR00083. HOLDHDRGNASE.
TIGRFAMs	TIGR00069. hisD. 1 hit.
PROSITE	PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HISX_BORPE

Accession

Primary (citable) accession number: Q7VSZ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	October 1, 2003
Last modified:	February 9, 2010
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)