Reviewed, UniProtKB/Swiss-Prot Q8YF59 (HISX_BRUME)

Names and origin

Protein names

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

Gene names

Name:	hisD
Ordered Locus Names:	BMEI1668

Organism

Brucella melitensis [Complete proteome] [HAMAP]

Taxonomic identifier

29459 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	430 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 – 430	430	Histidinol dehydrogenase		PRO_0000135740
Sites
	Active site	327	1	Proton acceptor By similarity
	Active site	328	1	Proton acceptor By similarity
	Metal binding	259	1	Zinc By similarity
	Metal binding	262	1	Zinc By similarity
	Metal binding	361	1	Zinc By similarity
	Metal binding	420	1	Zinc By similarity
	Binding site	130	1	NAD By similarity
	Binding site	191	1	NAD By similarity
	Binding site	214	1	NAD By similarity
	Binding site	237	1	Substrate By similarity
	Binding site	259	1	Substrate By similarity
	Binding site	262	1	Substrate By similarity
	Binding site	328	1	Substrate By similarity
	Binding site	361	1	Substrate By similarity
	Binding site	415	1	Substrate By similarity
	Binding site	420	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8YF59-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 21765279719C8FE0	FASTA	430	46,071
	10 20 30 40 50 60 MVTTLRQTDP DFEQKFAAFL SGKREVSEDV DRAVREIVDR VRREGDSALL DYSRRFDRID 70 80 90 100 110 120 LEKTGIAVTE AEIDAAFDAA PASTVEALKL ARDRIEKHHA RQLPKDDRYT DALGVELGSR 130 140 150 160 170 180 WTAIKAVGLY VPGGTASYPS SVLMNAMPAK VAGVDRIVMV VPAPDGNLNP LVLVAARLAG 190 200 210 220 230 240 VSEIYRVGGA QAIAALAYGT ETIRPVAKIV GPGNAYVAAA KRIVFGTVGI DMIAGPSEVL 250 260 270 280 290 300 IVADKDNNPD WIAADLLAQA EHDTAAQSIL MTNDEAFAHA VEEAVERQLH TLARTETASA 310 320 330 340 350 360 SWRDFGAVIL VKDFEDAIPL ANRIAAEHLE IAVADAEAFV PRIRNAGSIF IGGYTPEVIG 370 380 390 400 410 420 DYVGGCNHVL PTARSARFSS GLSVLDYMKR TSLLKLGSEQ LRALGPAAIE IARAEGLDAH 430 AQSVAIRLNL

References

[1]

"The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. , Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., Haselkorn R., Kyrpides N.C., Overbeek R. Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed: 11756688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094 / Biotype 1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE009602 Genomic DNA. Translation: AAL52849.1.
PIR	AF3460.
RefSeq	NP_540585.1.
3D structure databases
HSSP	HSSP built from PDB template 1KAE based on UniProtKB P06988.
ModBase	Search...
Genome annotation databases
GeneID	1197379.
GenomeReviews	Gene locus BMEI1668 in contig AE008917_GR.
KEGG	bme:BMEI1668.
NMPDR	fig|224914.1.peg.1667.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8YF59.
Enzyme and pathway databases
BioCyc	BMEL224914:BMEI1668-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_BRUME

Accession

Primary (citable) accession number: Q8YF59

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	March 1, 2002
Last modified:	November 25, 2008
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)