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Q8TXG3 (HISX_METKA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:MK0711
OrganismMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) [Reference proteome] [HAMAP]
Taxonomic identifier190192 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus

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_0000135895

Sites

Active site3291Proton acceptor By similarity
Active site3301Proton acceptor By similarity
Metal binding2601Zinc By similarity
Metal binding2631Zinc By similarity
Metal binding3631Zinc By similarity
Metal binding4221Zinc By similarity
Binding site1271NAD By similarity
Binding site1901NAD By similarity
Binding site2131NAD By similarity
Binding site2381Substrate By similarity
Binding site2601Substrate By similarity
Binding site2631Substrate By similarity
Binding site3301Substrate By similarity
Binding site3631Substrate By similarity
Binding site4171Substrate By similarity
Binding site4221Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8TXG3 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 50DD46829C9EB5DC

FASTA43147,335
        10         20         30         40         50         60 
MRLLVRPEEE ELERVLRRSE MDVTEVLPDV ERIFEDVVER GDEALLEYTE RFDGVKLEAE 

        70         80         90        100        110        120 
DLRVSEDDFE VARELVDERT VEALEEAAHR IEEFHRKTLP RVDRITFDVE GTECGLTLRP 

       130        140        150        160        170        180 
IPRVGCYVPG GRAAYPSTAL MTVIPARVAG CREVVVCTPP ADNDVRASPE VLVAVEIAGA 

       190        200        210        220        230        240 
DAVYRVGGAQ AIAALAAGTE TVLRVDKIVG PGNVYVTAAK LLAYSRGLTD VDMPAGPSEV 

       250        260        270        280        290        300 
FVIADDSANP DWLARDLIAQ AEHDPHAAAV LATDSEEIAR AVKERVEELL DAGIEREEIV 

       310        320        330        340        350        360 
LKALDRNGWI VVLDSLEECV RLANRYAPEH LQLCVENPEE LLQDVENAGA VFVGHLTAVP 

       370        380        390        400        410        420 
FGDYATGPNH VLPTGGFARA RGALGTWDFV KIIPIQRLRE GDVERLAPIV EELAEREGLP 

       430 
NHAEAVRARR S 

« Hide

References

[1]"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009439 Genomic DNA. Translation: AAM01925.1.
RefSeqNP_613995.1. NC_003551.1.

3D structure databases

ProteinModelPortalQ8TXG3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190192.MK0711.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM01925; AAM01925; MK0711.
GeneID1476812.
KEGGmka:MK0711.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.

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_METKA
AccessionPrimary (citable) accession number: Q8TXG3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: June 1, 2002
Last modified: February 19, 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