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Q3SW26 (HISX_NITWN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. 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:Nwi_0247
OrganismNitrobacter winogradskyi (strain Nb-255 / ATCC 25391) [Complete proteome] [HAMAP]
Taxonomic identifier323098 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter

Protein attributes

Sequence length429 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.

Sequence caution

The sequence ABA03515.1 differs from that shown. Reason: Erroneous initiation.

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 – 429429Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135803

Sites

Active site3271Proton acceptor By similarity
Active site3281Proton acceptor By similarity
Metal binding2591Zinc By similarity
Metal binding2621Zinc By similarity
Metal binding3611Zinc By similarity
Metal binding4201Zinc By similarity
Binding site1301NAD By similarity
Binding site1911NAD By similarity
Binding site2141NAD By similarity
Binding site2371Substrate By similarity
Binding site2591Substrate By similarity
Binding site2621Substrate By similarity
Binding site3281Substrate By similarity
Binding site3611Substrate By similarity
Binding site4151Substrate By similarity
Binding site4201Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3SW26 [UniParc].

Last modified January 10, 2006. Version 2.
Checksum: AED2E80E595F7F0C

FASTA42944,496
        10         20         30         40         50         60 
MPIRIDSRNA DFVPRFKAFL ATKREVSADI EAATRAIVDD VAARGDAALI EATCKFDRLS 

        70         80         90        100        110        120 
VDAAGLRFTA AEIDAAVAAC DAATLDALKL ARDRIETFHR RQLPKDDRFI DALGVELGSR 

       130        140        150        160        170        180 
WTAIEAVGLY VPGGSAAYPS SVLMNAVPAM VAGVARVVMV VPSPAGRINP LVLAAARLGG 

       190        200        210        220        230        240 
VSEIYRVGGA QAVAALAYGT ATIAPVAKIV GPGNAYVAAA KRQVFGKVGI DMIAGPSEVL 

       250        260        270        280        290        300 
VIADQTGNAG WIAADLLAQA EHDANAQSIL ITDSEALAAD VERAVETQLA TLPRAGIARA 

       310        320        330        340        350        360 
SWNDFGAVIL VTDLDEAVVL ADSIAAEHLE IMTADPEGLA ARIRNAGAIF LGPHTPEAIG 

       370        380        390        400        410        420 
DYVGGSNHVL PTARSARFSS GLGVLDFMKR TSILKCGPDQ LRALGPAAMT LGKAEGLDAH 


ARSVGVRLN 

« Hide

References

[1]"Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium Nitrobacter winogradskyi Nb-255."
Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J., Hickey W.J.
Appl. Environ. Microbiol. 72:2050-2063(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nb-255 / ATCC 25391.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000115 Genomic DNA. Translation: ABA03515.1. Different initiation.
RefSeqYP_316867.1. NC_007406.1.

3D structure databases

ProteinModelPortalQ3SW26.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323098.Nwi_0247.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA03515; ABA03515; Nwi_0247.
GeneID3674153.
KEGGnwi:Nwi_0247.
PATRIC22696844. VBINitWin102302_0273.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycNWIN323098:GJEG-252-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_NITWN
AccessionPrimary (citable) accession number: Q3SW26
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: May 14, 2014
This is version 63 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