Reviewed, UniProtKB/Swiss-Prot O34651 (HISX_BACSU)

Names and origin

Protein names

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

Gene names

Name:	hisD
Ordered Locus Names:	BSU34910

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	427 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. HAMAP MF_01024
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. 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 – 427	427	Histidinol dehydrogenase HAMAP MF_01024		PRO_0000135728
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)
	O34651-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: BDB0B2AE3C580E7F	FASTA	427	46,256
	10 20 30 40 50 60 MKIKTISGAE RLSLKRSIDA GTEEQRKTVR SIIEDVKANG DQAVRSYTAK FDCIEIDSPL 70 80 90 100 110 120 VTKEEFEEAY TSLDSRLLQV IRQAIENIRE YHERQLQSSW FYHRKDGTML GQKVTALDSA 130 140 150 160 170 180 GVYVPGGTAA YPSSVLMNVI PALVAGVERI VLVTPPGKDG LLSPGVLVAA AELGIKDIYK 190 200 210 220 230 240 MGGAQAIAAL AYGTETIEPV DKITGPGNIY VALAKREVFG DVDIDMIAGP SEIVVLADET 250 260 270 280 290 300 AIPSEIAADL LSQAEHDKLS SCVFVTDSMA LAETVSAEVN KQLETLPRRE IAEASVRDYG 310 320 330 340 350 360 CIYVAETMVE AIETVNTLAP EHLEIITQSP EALLGSIKHA GAIFLGRYSP EPVGDYFAGP 370 380 390 400 410 420 NHVLPTNGTA RFSSPLNVTD FQKKSSIISY SQSAFEEHAE SIAAFARLEG LEAHARSIEA RERRISK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the 300-304 chromosomal segment of Bacillus subtilis." Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF017113 Genomic DNA. Translation: AAC67295.1. AL009126 Genomic DNA. Translation: CAB15496.1.
PIR	A69641.
RefSeq	NP_391371.1.
3D structure databases
HSSP	HSSP built from PDB template 1K75 based on UniProtKB P06988.
ModBase	Search...
Genome annotation databases
GeneID	936584.
GenomeReviews	Gene locus BSU34910 in contig AL009126_GR.
KEGG	bsu:BSU34910.
NMPDR	fig|224308.1.peg.3497.
Organism-specific databases
SubtiList	BG12599. hisD. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	O34651.
OMA	LDAHKNA.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3488-MON.
BRENDA	1.1.1.23. 150.
Family and domain databases
HAMAP	MF_01024. [Tree]
InterPro	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.
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_BACSU

Accession

Primary (citable) accession number: O34651

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 69 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)