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Q8DGR2 (HISX_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 80. 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:tll2252
OrganismThermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length431 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 – 431431Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135862

Sites

Active site3281Proton acceptor By similarity
Active site3291Proton acceptor By similarity
Metal binding2601Zinc By similarity
Metal binding2631Zinc By similarity
Metal binding3621Zinc By similarity
Metal binding4211Zinc By similarity
Binding site1301NAD By similarity
Binding site1921NAD By similarity
Binding site2151NAD By similarity
Binding site2381Substrate By similarity
Binding site2601Substrate By similarity
Binding site2631Substrate By similarity
Binding site3291Substrate By similarity
Binding site3621Substrate By similarity
Binding site4161Substrate By similarity
Binding site4211Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DGR2 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E94C15E8A677677A

FASTA43146,340
        10         20         30         40         50         60 
MLRIITQLTD LRAELRRICD RTDSGEMSEQ QATVEAILRR VAKDGDRALI EYTAQFDHID 

        70         80         90        100        110        120 
LTPETLRVKG DELDAAYQQV SKELLDAIRL AKQQIEAFHR QRVPKSWVQF GEDGVVLGKR 

       130        140        150        160        170        180 
YTAVDAAGLY VPGGRAAYPS TVLMNAIPAQ VAGVQRIVMV TPPGQGKGIN PAVLVAAQEA 

       190        200        210        220        230        240 
GIQEIYRVGG AQAIAALAYG TETIPRVDVI TGPGNLYVML AKKQVYGRVG IDSLAGPSEV 

       250        260        270        280        290        300 
LIIADEAAHP AQIAADLLAQ AEHDPLAAAI LLTPSLSLAK AVVTAVNEQL ADHPRRVLTE 

       310        320        330        340        350        360 
KAIAHYGLIG IVETLEQAVE LSNSFAPEHL ELEVEDPWSL VEQVRHAGAI FLGYSTPEAV 

       370        380        390        400        410        420 
GDYLAGPNHT LPTSGAARYA SALGVETFLK HSSIIQYTPA ALRKQGGAVM TLAETEGLIS 

       430 
HRDSVRLRLQ P 

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000039 Genomic DNA. Translation: BAC09804.1.
RefSeqNP_683042.1. NC_004113.1.

3D structure databases

ProteinModelPortalQ8DGR2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING197221.tll2252.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC09804; BAC09804; BAC09804.
GeneID1012296.
KEGGtel:tll2252.
PATRIC23929958. VBITheElo119873_2360.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAYAAKLCG.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

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_THEEB
AccessionPrimary (citable) accession number: Q8DGR2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 80 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