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O59626 (HISX_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 97. 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:PF1659
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

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
Reference 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_0000135903

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

Experimental info

Sequence conflict971G → R in BAA25804. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O59626 [UniParc].

Last modified April 3, 2002. Version 2.
Checksum: F8874116A40B1A1B

FASTA37542,178
        10         20         30         40         50         60 
MDIEEYVREI LKDIRERGLE AIREYSKKFD GYEGPFEVSK EEFKEAEERI PERDKEIIKR 

        70         80         90        100        110        120 
TLKRIEKYHR KQLKQDILYI ENGSLYGLIY KPLKRIGIYV PGGKPLPSTL MMVGVPARVA 

       130        140        150        160        170        180 
GVKEIVVTNP PKDGKVNPYI LYIAKLLKIE EVYKLGGIQA IAAMAYGIGM KKVQKIFGPG 

       190        200        210        220        230        240 
NKFVNEAKRQ VFGIVGIDSL AGPSEIAVIA DESADKDFVL YDLLSQLEHG KDSKAWLLTT 

       250        260        270        280        290        300 
SKELADYCNR EGITVIVCSS LEECCKKANE IAPEHLEIIT REPLKLVDLI ENAGAIYLGL 

       310        320        330        340        350        360 
YTPVPAADYF LGVNHVLPTG GAAKFMGVLT VWDFMKPISI AMVSREEFIS ERELGIRLAE 

       370 
IEGIELHKKS LEVRK 

« Hide

References

« Hide 'large scale' references
[1]Kanai A., Oida H., Hasegawa A., Doi H.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB013080 Genomic DNA. Translation: BAA25804.1.
AE009950 Genomic DNA. Translation: AAL81783.1.
RefSeqNP_579388.1. NC_003413.1.

3D structure databases

ProteinModelPortalO59626.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186497.PF1659.

Proteomic databases

PRIDEO59626.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL81783; AAL81783; PF1659.
GeneID1469536.
KEGGpfu:PF1659.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMANAMSILL.

Enzyme and pathway databases

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_PYRFU
AccessionPrimary (citable) accession number: O59626
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: April 3, 2002
Last modified: May 14, 2014
This is version 97 of the entry and version 2 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