Reviewed, UniProtKB/Swiss-Prot Q7W2Y4 (HISX_BORPA)

Names and origin

Protein names

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

Gene names

Name:	hisD
Ordered Locus Names:	BPP4267

Organism

Bordetella parapertussis [Complete proteome] [HAMAP]

Taxonomic identifier

519 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	440 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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 binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 440	440	Histidinol dehydrogenase		PRO_0000135737
Sites
	Active site	336	1	Proton acceptor By similarity
	Active site	337	1	Proton acceptor By similarity
	Metal binding	268	1	Zinc By similarity
	Metal binding	271	1	Zinc By similarity
	Metal binding	370	1	Zinc By similarity
	Metal binding	429	1	Zinc By similarity
	Binding site	139	1	NAD By similarity
	Binding site	200	1	NAD By similarity
	Binding site	223	1	NAD By similarity
	Binding site	246	1	Substrate By similarity
	Binding site	268	1	Substrate By similarity
	Binding site	271	1	Substrate By similarity
	Binding site	337	1	Substrate By similarity
	Binding site	370	1	Substrate By similarity
	Binding site	424	1	Substrate By similarity
	Binding site	429	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7W2Y4-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: D8FC76AF462F129A	FASTA	440	46,882
	10 20 30 40 50 60 MQYHDAMALI NRLDSRDPGF KTALSQLLAF EAEQDESIDQ AAAGILADVR RRGDAALLEY 70 80 90 100 110 120 TQRFDRLAVD DATALEIPQA DWHAALDSLP AAQRQALEAA AARVRAYHER QRGETWTYTE 130 140 150 160 170 180 ADGTMLGQQI TALDRVGLYV PGGKAAYPSS VLMNAIPAKV AGVPELIMVT PTPDGVRNPI 190 200 210 220 230 240 VLAAAAIAGV DRAFAIGGAQ AVGALAYGTA TVPAVDKIVG PGNAYVAAAK RRVFGTVGID 250 260 270 280 290 300 MIAGPSEILV ICDGKTPADW IAMDLFSQAE HDELAQSILL CPDAAFLAEV EAAIERLLPG 310 320 330 340 350 360 MPRADILRVS LANRGALILV RDLEEACAIA NDIAPEHLEI STEQPQRWTA LIRHAGAIFM 370 380 390 400 410 420 GRYSSEALGD YCAGPNHVLP TSRTARFSSP LGVYDFQKRS SLIQVSREGA QTLGRIAAEL 430 440 ALGEGLQAHA ASAQYRLDQP

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: 12822 / ATCC BAA-587 / NCTC 13253.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640436 Genomic DNA. Translation: CAE39546.1.
RefSeq	NP_886396.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1667362.
GenomeReviews	Gene locus BPP4267 in contig BX470249_GR.
KEGG	bpa:BPP4267.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7W2Y4.
Enzyme and pathway databases
BioCyc	BPAR257311:BPP4267-MON.
Family and domain databases
HAMAP	MF_01024. [Tree]
InterPro	IPR001692. Histidinol_DHase. IPR012131. Hstdl_DHase_prok. IPR002035. VWF_A. [Graphical view]
PANTHER	PTHR21256:SF2. Hstdl_DH_prok. 1 hit.
Pfam	PF00815. Histidinol_dh. 1 hit. [Graphical view]
PRINTS	PR00083. HOLDHDRGNASE. PR00453. VWFADOMAIN.
ProDom	PD002680. Histidinol_dh. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00069. hisD. 1 hit.
PROSITE	PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HISX_BORPA

Accession

Primary (citable) accession number: Q7W2Y4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	October 1, 2003
Last modified:	November 25, 2008
This is version 37 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)