Reviewed, UniProtKB/Swiss-Prot P62456 (HISX_BACC1)

Names and origin

Protein names

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

Gene names

Name:	hisD
Ordered Locus Names:	BCE_1526

Organism

Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]

Taxonomic identifier

222523 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	429 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 – 429	429	Histidinol dehydrogenase		PRO_0000135721
Sites
	Active site	324	1	Proton acceptor By similarity
	Active site	325	1	Proton acceptor By similarity
	Metal binding	256	1	Zinc By similarity
	Metal binding	259	1	Zinc By similarity
	Metal binding	358	1	Zinc By similarity
	Metal binding	417	1	Zinc By similarity
	Binding site	127	1	NAD By similarity
	Binding site	188	1	NAD By similarity
	Binding site	211	1	NAD By similarity
	Binding site	234	1	Substrate By similarity
	Binding site	256	1	Substrate By similarity
	Binding site	259	1	Substrate By similarity
	Binding site	325	1	Substrate By similarity
	Binding site	358	1	Substrate By similarity
	Binding site	412	1	Substrate By similarity
	Binding site	417	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P62456-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: FBA64A1F6C18A30A	FASTA	429	47,360
	10 20 30 40 50 60 MEIVFEDFQK ALSKIKLLRE NANIIEETVQ RNVSEIVRNV RESGDEALSF YTKKFDGVKI 70 80 90 100 110 120 KEFRVSEEEE KRASMFVENS FLEALQEAKK NIISYHEKQK RQSMFDCASE GIIRGQIIRP 130 140 150 160 170 180 LENVGVYVPG GTASYPSSVL MNVLPAKLAG VKKIVMVTPP REGGIDPHIL VAASLAGVDE 190 200 210 220 230 240 IYTIGGAQAI AALAYGTESI PKVDKIVGPG NLYVALAKRE VYGIVNIDMI AGPSEIVVIA 250 260 270 280 290 300 DETGNAKYIA ADLLSQAEHD ERATAICITT NIELAKKVEK EIERQLETLP RSEIARESIN 310 320 330 340 350 360 RNGAIFIVPS IDEALQLSNE IAPEHLELHI KEPMNALAYV KHAGSIFLGP YAPEPLGDYL 370 380 390 400 410 420 AGPNHVLPTS GTARFFSPLS VDDFVKKSSF LSYTEEALRD VQHHIVELAN KEGLHAHARA IQIRFEEEE

References

[1]

"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017194 Genomic DNA. Translation: AAS40455.1.
RefSeq	NP_977847.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2748395.
GenomeReviews	Gene locus BCE_1526 in contig AE017194_GR.
KEGG	bca:BCE_1526.
NMPDR	fig|222523.1.peg.1519.
TIGR	BCE_1526.
Phylogenomic databases
HOGENOM	P62456.
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_BACC1

Accession

Primary (citable) accession number: P62456

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	July 5, 2004
Last modified:	November 25, 2008
This is version 39 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)