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Q9RQ88 (HISX_BUCDN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 60. 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. Diuraphis noxia
Taxonomic identifier118101 [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_0000135744

Experimental info

Non-terminal residue2011

Sequences

Sequence LengthMass (Da)Tools
Q9RQ88 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 24DD9DAED0371334

FASTA20122,605
        10         20         30         40         50         60 
MNYLKNIFYW SKLNYDEQQK ILSRPILNRN HTVKDTVKKV IENVKNFGDN ALRKYSILFD 

        70         80         90        100        110        120 
KFNVNEFRIP EEKIISSFLN INENLKSSIL IAKKNITSFH EAQILSTIDI ETQIGVRCQQ 

       130        140        150        160        170        180 
VYLPLNSVGI YIPNGTTSLF SSVLMLAIPA KIAGCKEIIL CSPPPINNNI LYASYVCGIK 

       190        200 
KIFQVGGAQA IAALAFGTET 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
AF129281 Genomic DNA. Translation: AAF13770.1.

3D structure databases

ProteinModelPortalQ9RQ88.
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_BUCDN
AccessionPrimary (citable) accession number: Q9RQ88
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 60 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