Reviewed, UniProtKB/Swiss-Prot Q63Q86 (HISX_BURPS)

Names and origin

Protein names

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

Gene names

Name:	hisD
Ordered Locus Names:	BPSL3139

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei) [Complete proteome] [HAMAP]

Taxonomic identifier

28450 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	445 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 – 445	445	Histidinol dehydrogenase		PRO_0000135750
Sites
	Active site	335	1	Proton acceptor By similarity
	Active site	336	1	Proton acceptor By similarity
	Metal binding	267	1	Zinc By similarity
	Metal binding	270	1	Zinc By similarity
	Metal binding	369	1	Zinc By similarity
	Metal binding	428	1	Zinc By similarity
	Binding site	138	1	NAD By similarity
	Binding site	199	1	NAD By similarity
	Binding site	222	1	NAD By similarity
	Binding site	245	1	Substrate By similarity
	Binding site	267	1	Substrate By similarity
	Binding site	270	1	Substrate By similarity
	Binding site	336	1	Substrate By similarity
	Binding site	369	1	Substrate By similarity
	Binding site	423	1	Substrate By similarity
	Binding site	428	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q63Q86-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 3E9BD760F554A7E8	FASTA	445	47,363
	10 20 30 40 50 60 MAIKIRKLDS TSEGFAAELR AVLAFEASED DAIERAVAQI LADVKARGDA AVLDYTNRFD 70 80 90 100 110 120 RLNAASVAAL ELPQSELEAA LEGLEPKRRA ALEAAAARVR GYHEKQKIEC GSHSWQYTEA 130 140 150 160 170 180 DGTVLGQKVT PLDRVGLYVP GGKAAYPSSV LMNAIPARVA GVGEIVMVVP TPDGLKNDLV 190 200 210 220 230 240 LAAALLGGVD RVFTIGGAQA VAALAYGTQT VPAVDKICGP GNAYVASAKR RVFGTVGIDM 250 260 270 280 290 300 IAGPSEILVL CDGTTDPSWV AMDLFSQAEH DELAQSILLC PDEAFIERVE KAIGELLPTM 310 320 330 340 350 360 PRQDVIRASL EGRGALVKVR DMAEACRIAN DIAPEHLEIS ALEPHQWGKQ IRHAGAIFLG 370 380 390 400 410 420 RYTSESLGDY CAGPNHVLPT SRTARFSSPL GVYDFFKRSS LIEVSAEGAH TLGEIASELA 430 440 YGEGLQAHAK SAEYRMKGAG DRQKG

References

[1]

"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX571965 Genomic DNA. Translation: CAH37149.1.
RefSeq	YP_109732.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3091925.
GenomeReviews	Gene locus BPSL3139 in contig BX571965_GR.
KEGG	bps:BPSL3139.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q63Q86.
Enzyme and pathway databases
BioCyc	BPSE272560:BPSL3139-MON.
Family and domain databases
HAMAP	MF_01024. [Tree]
InterPro	IPR001692. Histidinol_DHase. IPR012131. Hstdl_DHase_prok. [Graphical view]
PANTHER	PTHR21256:SF2. Hstdl_DH_prok. 1 hit.
Pfam	PF00815. Histidinol_dh. 1 hit. [Graphical view]
PRINTS	PR00083. HOLDHDRGNASE.
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_BURPS

Accession

Primary (citable) accession number: Q63Q86

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	October 25, 2004
Last modified:	November 25, 2008
This is version 35 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)