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Q58851 (HISX_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:MJ1456
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length429 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 – 429429Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135894

Sites

Active site3271Proton acceptor By similarity
Active site3281Proton acceptor By similarity
Metal binding2611Zinc By similarity
Metal binding2641Zinc By similarity
Metal binding3611Zinc By similarity
Metal binding4201Zinc By similarity
Binding site1311NAD By similarity
Binding site1931NAD By similarity
Binding site2161NAD By similarity
Binding site2391Substrate By similarity
Binding site2611Substrate By similarity
Binding site2641Substrate By similarity
Binding site3281Substrate By similarity
Binding site3611Substrate By similarity
Binding site4151Substrate By similarity
Binding site4201Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q58851 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5E4DF4B17699EDB8

FASTA42947,433
        10         20         30         40         50         60 
MVTGMIIKKI KELTKEEEEK IINRNKANFE EILPTVMEIL KDVKEKGDEA LKYYTKKFDG 

        70         80         90        100        110        120 
VEIEDFKVTD EEIEEAYNSV DYKVVEAIER AKENIYFFHK KQMEQIKDLN VENNGIILGQ 

       130        140        150        160        170        180 
VVRAIEKVGC YVPGGRAFYP STVLMTTIPA KVAGCEEIYI TSPPTKDGKG NPATLIAGDI 

       190        200        210        220        230        240 
VGVSAIYKVG GVQAIGALAY GTETIPKVDI IVGPGNIYVT TAKKMVYGEV AIDFLAGPSE 

       250        260        270        280        290        300 
VLIIADETAN AEFVALDFIA QAEHDPNASC VITTTSEKKA EEIKNKIFEE IEKAERKEII 

       310        320        330        340        350        360 
LKALENSAIL IGDLEECIEF SNKYAPEHLE ILTKNPEEVL NKIKHAGSVF LGEYSPVPVG 

       370        380        390        400        410        420 
DYASGTNHVL PTSQFARMSS GLNVETFLKK ITYQKLDKES LKNIADIVIT LAEAEGLFGH 


AEAVRRRLK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB99465.1.
PIRG64481.
RefSeqNP_248460.1. NC_000909.1.

3D structure databases

ProteinModelPortalQ58851.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ1456.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB99465; AAB99465; MJ_1456.
GeneID1452360.
KEGGmja:MJ_1456.

Phylogenomic databases

eggNOGCOG0141.
KOK00013.
OMAYAAKLCG.
PhylomeDBQ58851.

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_METJA
AccessionPrimary (citable) accession number: Q58851
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 98 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

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names