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Q6KZD1 (HISX_PICTO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidinol dehydrogenase

Short name=HDH
EC=1.1.1.23
Gene names
Name:hisD
Ordered Locus Names:PTO1336
OrganismPicrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828) [Complete proteome] [HAMAP]
Taxonomic identifier263820 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesPicrophilaceaePicrophilus

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Protein existenceInferred 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-Rule MF_01024

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP-Rule MF_01024

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP-Rule MF_01024

Sequence similarities

Belongs to the histidinol dehydrogenase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

histidinol dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135901

Sites

Active site2741Proton acceptor By similarity
Active site2751Proton acceptor By similarity
Metal binding2261Zinc By similarity
Metal binding2291Zinc By similarity
Metal binding3081Zinc By similarity
Metal binding3671Zinc By similarity
Binding site991NAD By similarity
Binding site1591NAD By similarity
Binding site1811NAD By similarity
Binding site2041Substrate By similarity
Binding site2261Substrate By similarity
Binding site2291Substrate By similarity
Binding site2751Substrate By similarity
Binding site3081Substrate By similarity
Binding site3621Substrate By similarity
Binding site3671Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6KZD1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 5DA4E83583844BD1

FASTA37541,836
        10         20         30         40         50         60 
MDIYEYVSNI ISDVRINGID ALKRYSEAFD NYSGGFTVTD DEIEDADKSI KPGEKDAIKN 

        70         80         90        100        110        120 
IYERIYEYHK NQFEGQKINI KNGSIYGIIY RPIDRIGLYV PGKRALPSTL MMLGIPARIA 

       130        140        150        160        170        180 
GVKSIVLCTA PENGNVNKYT LYIARLLGIR EIYKIGGVQA IAAMAYGISM KPVDKIFGPG 

       190        200        210        220        230        240 
NKYVNEAKRQ VFGITGIDGL YGPSEICLIA DDSANINYIK NDLLSQLEHG EASSAYLITN 

       250        260        270        280        290        300 
SLRIYNEVKL ENVKKYYKET VEESIELANE IAPEHLELLV NDPLKYLNII RNAGAVYMGE 

       310        320        330        340        350        360 
YGPVPAGDYF LGVNHVLPTG SSARFSSVLT VYDFMKRISV AMPSKYDFLS AVDSGLKLAS 

       370 
IENMKMHYKS MEARI 

« Hide

References

[1]"Genome sequence of Picrophilus torridus and its implications for life around pH 0."
Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C., Schepers B., Dock C., Antranikian G., Liebl W.
Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017261 Genomic DNA. Translation: AAT43921.1.
RefSeqYP_024114.1. NC_005877.1.

3D structure databases

ProteinModelPortalQ6KZD1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING263820.PTO1336.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT43921; AAT43921; PTO1336.
GeneID2844768.
KEGGpto:PTO1336.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMANAMSILL.

Enzyme and pathway databases

BioCycPTOR263820:GHA3-1385-MONOMER.
UniPathwayUPA00031; UER00014.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR012131. Hstdl_DH.
[Graphical view]
PfamPF00815. Histidinol_dh. 2 hits.
[Graphical view]
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHISX_PICTO
AccessionPrimary (citable) accession number: Q6KZD1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways