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Q9RSI4 (HISX_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 93. 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:DR_2140
OrganismDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]
Taxonomic identifier243230 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

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
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 – 436436Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135766

Sites

Active site3341Proton acceptor By similarity
Active site3351Proton acceptor By similarity
Metal binding2651Zinc By similarity
Metal binding2681Zinc By similarity
Metal binding3681Zinc By similarity
Metal binding4271Zinc By similarity
Binding site1351NAD By similarity
Binding site1971NAD By similarity
Binding site2201NAD By similarity
Binding site2431Substrate By similarity
Binding site2651Substrate By similarity
Binding site2681Substrate By similarity
Binding site3351Substrate By similarity
Binding site3681Substrate By similarity
Binding site4221Substrate By similarity
Binding site4271Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RSI4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: FB3A68DF7457E6B2

FASTA43646,273
        10         20         30         40         50         60 
MQVLQGAEAR AALTRTFSQI PVPDAVLSRI EQTFGERLTP EQVVERILLD VRARGDDALR 

        70         80         90        100        110        120 
DWTERLDGPR PAELEVPAAE LEAAQVAPEL HAAIRLAAER VRAFYRQQPA HGFLEHGPDG 

       130        140        150        160        170        180 
ALGQLVRPLG RVGVYVPGGL APLISTLMHT AVPAQVAGVP DIVVTTPPGK DGQVHPAILV 

       190        200        210        220        230        240 
AARELGLSRV FKVGGAQAIA ALAYGTASVP AVDKIAGPGN LFVVIAKRLV YGQTGIESLP 

       250        260        270        280        290        300 
GPTETLVVAD DSASPRYVAA DLLAQAEHNG AEPVLVSVSR ELLLAVQAEL NEQLENLPEP 

       310        320        330        340        350        360 
NRSWARDSVG ARMKVVLADS LDEALDLANL YAPEHLCLLT RDPWSLLGQV RRAGGVFVGE 

       370        380        390        400        410        420 
ASMEALGDYV AGPSHVMPTG GTARFMSPVN VRDFQNIISV VGVNEETLRR IGPAAATLAR 

       430 
AEGLEAHARA VESRLK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000513 Genomic DNA. Translation: AAF11684.1.
PIRA75311.
RefSeqNP_295863.1. NC_001263.1.

3D structure databases

ProteinModelPortalQ9RSI4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243230.DR_2140.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF11684; AAF11684; DR_2140.
GeneID1800305.
KEGGdra:DR_2140.
PATRIC21631956. VBIDeiRad64572_2363.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.
ProtClustDBCLSK986476.

Enzyme and pathway databases

BioCycDRAD243230:GH46-2183-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_DEIRA
AccessionPrimary (citable) accession number: Q9RSI4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 93 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