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Q67KH6 (HISX_SYMTH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. 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:STH2837
OrganismSymbiobacterium thermophilum (strain T / IAM 14863) [Complete proteome] [HAMAP]
Taxonomic identifier292459 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiales Family XVIII. Incertae SedisSymbiobacterium

Protein attributes

Sequence length439 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 – 439439Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135861

Sites

Active site3231Proton acceptor By similarity
Active site3241Proton acceptor By similarity
Metal binding2551Zinc By similarity
Metal binding2581Zinc By similarity
Metal binding3571Zinc By similarity
Metal binding4161Zinc By similarity
Binding site1251NAD By similarity
Binding site1871NAD By similarity
Binding site2101NAD By similarity
Binding site2331Substrate By similarity
Binding site2551Substrate By similarity
Binding site2581Substrate By similarity
Binding site3241Substrate By similarity
Binding site3571Substrate By similarity
Binding site4111Substrate By similarity
Binding site4161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q67KH6 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 45D8E26BC3568EAA

FASTA43946,628
        10         20         30         40         50         60 
MLKVWEPQAF LEFLNRRRTE FYPEIEAQVR AILERVRREG DGALYAFTRQ FDGADLEATG 

        70         80         90        100        110        120 
LRVTEAEYRE AEAAVSAAFR AALQVAVENI AAFHRPQVPT SWFTTRPDGT IVGQRVTPVD 

       130        140        150        160        170        180 
RAGVYVPGGS APLFSCLLMT AIPAVVAGVP EVIVCTPPDR NGRIDPHMLV AARAAGVKDV 

       190        200        210        220        230        240 
YKVGGAQAIG AMAYGTATVP RVDKIAGPGN YYVTLAKKLV FGPVGIDMLA GPTEVMAVDD 

       250        260        270        280        290        300 
GSVDAEWLAA DLLSQAEHPN GMVILVTTAG PERIAAVGAA MARHTAALPR AETIRRSVAE 

       310        320        330        340        350        360 
LGAALAVDTL EEAADLVNAV GPEHLEVGVA DPWAFLPLVR HAGSIFLGRW TPEAMGDYIA 

       370        380        390        400        410        420 
GPSNVIPTEG TARYASPVCV ETFIKRSAVT CYSEAAFRAQ APHAVRLALT EDLLAHAASM 

       430 
QIRLAKPDGE SPSEGREAG 

« Hide

References

[1]"Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism."
Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.
Nucleic Acids Res. 32:4937-4944(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T / IAM 14863.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006840 Genomic DNA. Translation: BAD41822.1.
RefSeqYP_076666.1. NC_006177.1.

3D structure databases

ProteinModelPortalQ67KH6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292459.STH2837.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD41822; BAD41822; STH2837.
GeneID2979878.
KEGGsth:STH2837.
PATRIC23783855. VBISymThe116959_2816.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycSTHE292459:GJMM-2938-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_SYMTH
AccessionPrimary (citable) accession number: Q67KH6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: October 11, 2004
Last modified: February 19, 2014
This is version 74 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