Reviewed, UniProtKB/Swiss-Prot Q8G2R2 (HISX_BRUSU)

Names and origin

Protein names

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

Gene names

Name:	hisD
Ordered Locus Names:	BR0252

Organism

Brucella suis [Complete proteome] [HAMAP]

Taxonomic identifier

29461 [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. 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 – 430	430	Histidinol dehydrogenase HAMAP MF_01024		PRO_0000135741
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)
	Q8G2R2-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 2752FA59731001E0	FASTA	430	46,072
	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 WTAIEAVGLY 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 Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330 / Biovar 1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014291 Genomic DNA. Translation: AAN29201.1.
RefSeq	NP_697286.1.
3D structure databases
HSSP	HSSP built from PDB template 1KAE based on UniProtKB P06988.
ModBase	Search...
Genome annotation databases
GeneID	1165911.
GenomeReviews	Gene locus BR0252 in contig AE014291_GR.
KEGG	bms:BR0252.
NMPDR	fig|204722.1.peg.243.
TIGR	BR0252.
Phylogenomic databases
HOGENOM	Q8G2R2.
OMA	Q8G2R2. LLPEMPR.
Enzyme and pathway databases
BioCyc	BSUI204722:BR_0252-MON.
BRENDA	1.1.1.23. 281610.
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_BRUSU

Accession

Primary (citable) accession number: Q8G2R2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 47 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)