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Q3Z878 (HISX_DEHM1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. 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:DET0844
OrganismDehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195) (Dehalococcoides ethenogenes (strain 195)) [Complete proteome] [HAMAP]
Taxonomic identifier243164 [NCBI]
Taxonomic lineageBacteriaChloroflexiDehalococcoidiaDehalococcoidalesDehalococcoidaceaeDehalococcoides

Protein attributes

Sequence length436 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 – 436436Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135764

Sites

Active site3341Proton acceptor By similarity
Active site3351Proton acceptor By similarity
Metal binding2661Zinc By similarity
Metal binding2691Zinc By similarity
Metal binding3681Zinc By similarity
Metal binding4271Zinc By similarity
Binding site1361NAD By similarity
Binding site1981NAD By similarity
Binding site2211NAD By similarity
Binding site2441Substrate By similarity
Binding site2661Substrate By similarity
Binding site2691Substrate By similarity
Binding site3351Substrate By similarity
Binding site3681Substrate By similarity
Binding site4221Substrate By similarity
Binding site4271Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3Z878 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: B5BDCD65764EA53F

FASTA43646,836
        10         20         30         40         50         60 
MEIIRGFAPA EKRLSRRDKA GFFLDETQRA ELAKRLGVDP EKAVNGIIDD IRKQGDKAVL 

        70         80         90        100        110        120 
EYTLKFDRAA ISKLEVSPAE IKQAAGEIPA ELFEALKLAA TQVRAYHHFQ KEAVWKAAEI 

       130        140        150        160        170        180 
MQGKQLIRPL ERVGLYVPGG KAFYPSTVLM TAIPAKEAGV DEIILVTPPG ADGKIPAPTL 

       190        200        210        220        230        240 
AAAYIAGVDK VFACGGAQAV AALAFGTKSI PKVDKICGPG NIFVTLAKKA VFGVVDIDGL 

       250        260        270        280        290        300 
QGPSEVLILA DQYANAEYCA SDILAQAEHD VLASPIMVTT SAELAKRVND IVETKAGSCA 

       310        320        330        340        350        360 
RKDIIRQSLR DNGLIAVVDN MDEAIKLANM YATEHLCLLV KDSEQYLSRI NHAGCIFYGE 

       370        380        390        400        410        420 
KASVVMGDYV AGPSHALPTS GTARFSSPLN ILDFVKYIDI VNVSKEEVTK LGKAAVTIAR 

       430 
AEGLECHAEA ALKRME 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000027 Genomic DNA. Translation: AAW39898.1.
RefSeqYP_181571.1. NC_002936.3.

3D structure databases

ProteinModelPortalQ3Z878.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243164.DET0844.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW39898; AAW39898; DET0844.
GeneID3229860.
KEGGdet:DET0844.
PATRIC21608747. VBIDehEth89364_0802.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAYAAKLCG.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycDETH243164:GJNF-845-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_DEHM1
AccessionPrimary (citable) accession number: Q3Z878
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: September 27, 2005
Last modified: May 14, 2014
This is version 68 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