Reviewed, UniProtKB/Swiss-Prot Q65EF9 (HISX_BACLD)

Names and origin

Protein names

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

Gene names

Name:	hisD
Ordered Locus Names:	BLi03736, BL03408

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	426 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 – 426	426	Histidinol dehydrogenase HAMAP MF_01024		PRO_0000135727
Sites
	Active site	321	1	Proton acceptor By similarity
	Active site	322	1	Proton acceptor By similarity
	Metal binding	253	1	Zinc By similarity
	Metal binding	256	1	Zinc By similarity
	Metal binding	355	1	Zinc By similarity
	Metal binding	414	1	Zinc By similarity
	Binding site	123	1	NAD By similarity
	Binding site	185	1	NAD By similarity
	Binding site	208	1	NAD By similarity
	Binding site	231	1	Substrate By similarity
	Binding site	253	1	Substrate By similarity
	Binding site	256	1	Substrate By similarity
	Binding site	322	1	Substrate By similarity
	Binding site	355	1	Substrate By similarity
	Binding site	409	1	Substrate By similarity
	Binding site	414	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q65EF9-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 76A087539E215CA8	FASTA	426	46,028
	10 20 30 40 50 60 MKIKSISGNT SVSLKRSIDA GTEEQRKAVR GIIEEVKKNG NAAVSAFTRQ FDGADVAGFR 70 80 90 100 110 120 VSEEEIKEAY SALEERDLEI IQAAIFNIKE YHERQLATSW FYHRKDGTML GQKITPLDSA 130 140 150 160 170 180 GVYVPGGTAA YPSSVLMNVI PALVAGVDRI VLASPPGKDG KLSAGVLAAA AELGVTEIYK 190 200 210 220 230 240 MGGAQAIAAL AYGTETITPV DKITGPGNIY VALAKREVFG QVDIDMIAGP SEIAILADST 250 260 270 280 290 300 ANYREIAADL LSQAEHDAMA SSILVTDSET LAESVLKEVY RQLEHLPRKE IARQSIDNYG 310 320 330 340 350 360 LIYVTETMNE AVSVINELAP EHLEILTVQP DALLGQIKHA GAIFLGRYSS EPVGDYFAGP 370 380 390 400 410 420 NHVLPTNGTA RFSSPLNVTD FQKRSSIISY SREAFRANAE KIAAFARLEG LEAHARAIES RNREED

References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017333 Genomic DNA. Translation: AAU42555.1. CP000002 Genomic DNA. Translation: AAU25184.1.
RefSeq	YP_080822.1. YP_093248.1.
3D structure databases
SMR	Q65EF9. Positions 13-423.
ModBase	Search...
Protein-protein interaction databases
STRING	Q65EF9.
Genome annotation databases
GeneID	3027872. 3100933.
GenomeReviews	Gene locus BLi03736 in contig AE017333_GR. Gene locus BL03408 in contig CP000002_GR.
KEGG	bld:BLi03736. bli:BL03408.
NMPDR	fig|279010.5.peg.3801.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0141.
HOGENOM	HBG329596.
OMA	LDAHKNA.
Enzyme and pathway databases
BioCyc	BLIC279010-1:BLI03736-MONOMER. BLIC279010:BL03408-MONOMER.
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_BACLD

Accession

Primary (citable) accession number: Q65EF9
Secondary accession number(s): Q62PX7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	October 25, 2004
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)