Reviewed, UniProtKB/Swiss-Prot Q63DX2 (HISX_BACCZ)

Names and origin

Protein names

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

Gene names

Name:	hisD
Ordered Locus Names:	BCE33L1291

Organism

Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]

Taxonomic identifier

288681 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	429 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 – 429	429	Histidinol dehydrogenase HAMAP MF_01024		PRO_0000135723
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)
	Q63DX2-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: EBF5F9843321CD2C	FASTA	429	47,271
	10 20 30 40 50 60 MEIVCEDFQK ALTKIKLLRE NANIIEETVQ RSVREIVQNV RESRDEALSF YTKKFDGVEI 70 80 90 100 110 120 KDVRVSEEEI KQASMFVESS FLEALQEAKK NIISYHEKQK RQSMFDCTSK GIIRGQIIRP 130 140 150 160 170 180 LENIGVYVPG GTASYPSSVL MNVLPAKLAG VKKIVMVTPP RAGGIDPHIL VAASLAGVDE 190 200 210 220 230 240 IYMIGGAQAI AALAYGTESI PKVDKIVGPG NLYVALAKRE VYGIVNIDMI AGPSEIVVIA 250 260 270 280 290 300 DETGNAKYIA ADLLSQAEHD ERATAICITT NIELAKEVEK EIERQLETLP RSEIARESIN 310 320 330 340 350 360 RNGAIFIVPS IDEALQLSNE IAPEHLELHI KEPMNALAYV KHAGSIFLGP YAPEPLGDYL 370 380 390 400 410 420 AGPNHVLPTS GTARFFSPLS VDDFVKKSSF LSYTEEALRD VKHHIVELAN KEGLHAHARS IQIRFGEEE

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000001 Genomic DNA. Translation: AAU18958.1.
RefSeq	YP_082890.1.
3D structure databases
SMR	Q63DX2. Positions 17-427.
ModBase	Search...
Protein-protein interaction databases
STRING	Q63DX2.
Genome annotation databases
GeneID	3023156.
GenomeReviews	Gene locus BCE33L1291 in contig CP000001_GR.
KEGG	bcz:BCZK1291.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0141.
HOGENOM	HBG329596.
OMA	LDAHKNA.
Enzyme and pathway databases
BioCyc	BCER288681:BCE33L1291-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_BACCZ

Accession

Primary (citable) accession number: Q63DX2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	October 25, 2004
Last modified:	February 9, 2010
This is version 42 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)