Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5P790 (HISX_AROAE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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:AZOSEA06980
ORF Names:ebA1299
OrganismAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum

Protein attributes

Sequence length438 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 – 438438Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135718

Sites

Active site3341Proton acceptor By similarity
Active site3351Proton acceptor By similarity
Metal binding2661Zinc By similarity
Metal binding2691Zinc By similarity
Metal binding3681Zinc By similarity
Metal binding4271Zinc By similarity
Binding site1371NAD By similarity
Binding site1981NAD By similarity
Binding site2211NAD By similarity
Binding site2441Substrate By similarity
Binding site2661Substrate By similarity
Binding site2691Substrate By similarity
Binding site3351Substrate By similarity
Binding site3681Substrate By similarity
Binding site4221Substrate By similarity
Binding site4271Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5P790 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 4416060B3F732E8A

FASTA43846,793
        10         20         30         40         50         60 
MTAPAAAIRR LDAREPEFLA TLDALLAFEG GADARIDAAV SEILRAVRTT GDAAVLEYTR 

        70         80         90        100        110        120 
RFDHLDVKSM VQLELSKSEL KAALDSLTVE QREALRVAAD RVRVYHERQR AESWDYVEAD 

       130        140        150        160        170        180 
GTRLGQKVTP LDRVGLYVPG GRASYPSSVL MNAIPAKVAG VGELIMVVPT PNGEKNPLVL 

       190        200        210        220        230        240 
AAAAITGVDR VFTIGGAQAV AALAYGTQTL PQVDKIVGPG NAYVAEAKRR VFGTVGIDMV 

       250        260        270        280        290        300 
AGPSEVLIIS DGSGQAGWVA MDLFAQAEHD ELAQSILLCT DAGFIDAVAA SIERLLPSMP 

       310        320        330        340        350        360 
RRETIAASLA NRGALIHVDS LEQACAIANR IAPEHLELSL DDAEPWIGRI RHAGAIFVGH 

       370        380        390        400        410        420 
WSVEALGDYC AGPNHVLPTM RSARFSSPLG VYDFQKRTSI VQISEAGAQT LGRVASILAR 

       430 
GEGLQAHARS AEMRLHDR 

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EbN1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR555306 Genomic DNA. Translation: CAI06821.1.
RefSeqYP_157722.1. NC_006513.1.

3D structure databases

ProteinModelPortalQ5P790.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING76114.ebA1299.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI06821; CAI06821; ebA1299.
GeneID3179686.
KEGGeba:ebA1299.
PATRIC20967489. VBIAroAro98752_0708.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycAARO76114:GJTA-714-MONOMER.
UniPathwayUPA00031; UER00014.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000099. Histidinol_dh. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHISX_AROAE
AccessionPrimary (citable) accession number: Q5P790
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 4, 2005
Last modified: February 19, 2014
This is version 69 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