Reviewed, UniProtKB/Swiss-Prot Q5LUS2 (HISX2_SILPO)

Names and origin

Protein names

Recommended name:
    Histidinol dehydrogenase 2
      Short name=HDH 2
    EC=1.1.1.23

Gene names

Name:	hisD2
Ordered Locus Names:	SPO0981

Organism

Silicibacter pomeroyi [Complete proteome] [HAMAP]

Taxonomic identifier

89184 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Silicibacter

Protein attributes

Sequence length	433 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 – 433	433	Histidinol dehydrogenase 2		PRO_0000135847
Sites
	Active site	319	1	Proton acceptor By similarity
	Active site	320	1	Proton acceptor By similarity
	Metal binding	249	1	Zinc By similarity
	Metal binding	252	1	Zinc By similarity
	Metal binding	353	1	Zinc By similarity
	Metal binding	412	1	Zinc By similarity
	Binding site	119	1	NAD By similarity
	Binding site	181	1	NAD By similarity
	Binding site	204	1	NAD By similarity
	Binding site	227	1	Substrate By similarity
	Binding site	249	1	Substrate By similarity
	Binding site	252	1	Substrate By similarity
	Binding site	320	1	Substrate By similarity
	Binding site	353	1	Substrate By similarity
	Binding site	407	1	Substrate By similarity
	Binding site	412	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5LUS2-1 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: B67DC5531FADA3A3	FASTA	433	45,353
	10 20 30 40 50 60 MTITVLKSAP GLPPAPQGDA ADVVQVMLAR LRAEGEAAAR DYAARLDGWS GEIVVSPDQV 70 80 90 100 110 120 ARASEQVPED LKTQIRYAHD NIRRFAEAQR ASALDFQTEL RPGLIAGQKQ IPLAAAGAYV 130 140 150 160 170 180 PGGRYAHIAS ALMSIATARA AGVGQITAVS PPQVGRGVHP AILYAMSLAG ADRILALGGV 190 200 210 220 230 240 QGVAALAFGL FGAPPADILV GPGNQFVAEA KRQLFGPVGI DMFAGPTDSL VIADSTADPL 250 260 270 280 290 300 TVAWDLVGQA EHGYNSPVWL VTDSAALAEA VLAHIPGCIA DLPEPNRSSA QAAWDALGEV 310 320 330 340 350 360 ILCTDREEMA ATADRYAPEH LHVQAADLDW WRGRLSAYGS LFLGELTTVA FGDKASGPNH 370 380 390 400 410 420 VLPTSGAARY TGGLSVHKFL KTVTWQQVAP QALPDLARAT ATISRAEGME GHARTADIRL 430 EKLRPTLRQV GTG

References

[1]

"Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine environment." Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M. , Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N. Nature 432:910-913(2004) [PubMed: 15602564] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700808 / DSM 15171 / DSS-3.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000031 Genomic DNA. Translation: AAV94285.1.
RefSeq	YP_166233.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3193830.
GenomeReviews	Gene locus SPO0981 in contig CP000031_GR.
KEGG	sil:SPO0981.
NMPDR	fig|246200.3.peg.1401.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5LUS2.
Enzyme and pathway databases
BioCyc	SPOM246200:SPO_0981-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

HISX2_SILPO

Accession

Primary (citable) accession number: Q5LUS2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	February 1, 2005
Last modified:	November 25, 2008
This is version 31 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)