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Q9RQ85 (HISX_BUCSC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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
OrganismBuchnera aphidicola subsp. Schlechtendalia chinensis
Taxonomic identifier118110 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length201 AA.
Sequence statusFragment.
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.

Catalytic activity

L-histidinol + H2O + 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.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the histidinol dehydrogenase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›201›201Histidinol dehydrogenase
PRO_0000135747

Experimental info

Non-terminal residue2011

Sequences

Sequence LengthMass (Da)Tools
Q9RQ85 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 9C0370E1A3894358

FASTA20122,668
        10         20         30         40         50         60 
MHNILEVIYW NKCSYERKKK ILSRPIISNR FLIRNKVKEI ISNVKSFGDR ALYNYTNVFD 

        70         80         90        100        110        120 
NINLKNIRVS EEDIVSSHLH VSKELKLAVE VAFKNIKKFH SKQNVGSFNL KVQDNIYCQQ 

       130        140        150        160        170        180 
IIRPIESIGL YIPNGSAPLL STVLMLAIPA NIAGCKRIML CSPPPIMNEI LYACKICEIK 

       190        200 
DVFQIGGAQA IAALGCGTET I 

« Hide

References

[1]"Sequence evolution in bacterial endosymbionts having extreme base compositions."
Clark M.A., Moran N.A., Baumann P.
Mol. Biol. Evol. 16:1586-1598(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF129282 Genomic DNA. Translation: AAF13773.1.

3D structure databases

ProteinModelPortalQ9RQ85.
SMRQ9RQ85. Positions 7-201.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00031; UER00014.

Family and domain databases

InterProIPR016161. Ald_DH/histidinol_DH.
IPR012131. Hstdl_DH.
[Graphical view]
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. SSF53720. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHISX_BUCSC
AccessionPrimary (citable) accession number: Q9RQ85
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 59 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