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Q5FS83 (HISX_GLUOX) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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:GOX0991
OrganismGluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) [Complete proteome] [HAMAP]
Taxonomic identifier290633 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconobacter

Protein attributes

Sequence length430 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 – 430430Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135776

Sites

Active site3261Proton acceptor By similarity
Active site3271Proton acceptor By similarity
Metal binding2581Zinc By similarity
Metal binding2611Zinc By similarity
Metal binding3601Zinc By similarity
Metal binding4191Zinc By similarity
Binding site1291NAD By similarity
Binding site1901NAD By similarity
Binding site2131NAD By similarity
Binding site2361Substrate By similarity
Binding site2581Substrate By similarity
Binding site2611Substrate By similarity
Binding site3271Substrate By similarity
Binding site3601Substrate By similarity
Binding site4141Substrate By similarity
Binding site4191Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5FS83 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: C00338F3F3F3274F

FASTA43045,736
        10         20         30         40         50         60 
MKRLDTSAAG FSEDFATLLA ARGSDERSVA EPVRAILADV RSRGDEALCD YTARFDRLTL 

        70         80         90        100        110        120 
PAEKLRISAE EIASEAARVP ADLMDALRTA ARRIETFHAA QMPKDLDFTD EDGIRLGMRW 

       130        140        150        160        170        180 
TPLDAVGLYV PGGKAAYPSS VLMNALPARV AGVKRLAMCV PSPDGVLNPL VLAAAQLCGV 

       190        200        210        220        230        240 
EEIYRIGGAQ AVGAMAFGTD LIAPVDRIVG PGNAYVAEAK RQVFGHVGID SIAGPSEVVV 

       250        260        270        280        290        300 
VADGQNDPRL VALDLLAQAE HDEQAQAILI TTDAAFAERA AEAVRKELET LPRTAIASKS 

       310        320        330        340        350        360 
WEDHGAIIVV RSLEEAAEIV NALAPEHLEV MLDAPRDFSA MIRHAGAIFM GRYCPEAVGD 

       370        380        390        400        410        420 
YVGGPNHVLP TSRTARFASG LSVFDFIKRT TTIEADEAGL RRIGPAGVAL AKAEGLDAHA 

       430 
LSLSVRLEKN 

« Hide

References

[1]"Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
Nat. Biotechnol. 23:195-200(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 621H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000009 Genomic DNA. Translation: AAW60763.1.
RefSeqYP_191419.1. NC_006677.1.

3D structure databases

ProteinModelPortalQ5FS83.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290633.GOX0991.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW60763; AAW60763; GOX0991.
GeneID3250206.
KEGGgox:GOX0991.
PATRIC32609758. VBIGluOxy81109_1251.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAYAAKLCG.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycGOXY290633:GHB3-989-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_GLUOX
AccessionPrimary (citable) accession number: Q5FS83
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: March 1, 2005
Last modified: May 14, 2014
This is version 67 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