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Q5LUS2 (HISX2_RUEPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 71. 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 2

Short name=HDH 2
EC=1.1.1.23
Gene names
Name:hisD2
Ordered Locus Names:SPO0981
OrganismRuegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) [Complete proteome] [HAMAP]
Taxonomic identifier246200 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria

Protein attributes

Sequence length433 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 – 433433Histidinol dehydrogenase 2 HAMAP-Rule MF_01024
PRO_0000135847

Sites

Active site3191Proton acceptor By similarity
Active site3201Proton acceptor By similarity
Metal binding2491Zinc By similarity
Metal binding2521Zinc By similarity
Metal binding3531Zinc By similarity
Metal binding4121Zinc By similarity
Binding site1191NAD By similarity
Binding site1811NAD By similarity
Binding site2041NAD By similarity
Binding site2271Substrate By similarity
Binding site2491Substrate By similarity
Binding site2521Substrate By similarity
Binding site3201Substrate By similarity
Binding site3531Substrate By similarity
Binding site4071Substrate By similarity
Binding site4121Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5LUS2 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: B67DC5531FADA3A3

FASTA43345,353
        10         20         30         40         50         60 
MTITVLKSAP GLPPAPQGDA ADVVQVMLAR LRAEGEAAAR DYAARLDGWS GEIVVSPDQV 

        70         80         90        100        110        120 
ARASEQVPED LKTQIRYAHD NIRRFAEAQR ASALDFQTEL RPGLIAGQKQ IPLAAAGAYV 

       130        140        150        160        170        180 
PGGRYAHIAS ALMSIATARA AGVGQITAVS PPQVGRGVHP AILYAMSLAG ADRILALGGV 

       190        200        210        220        230        240 
QGVAALAFGL FGAPPADILV GPGNQFVAEA KRQLFGPVGI DMFAGPTDSL VIADSTADPL 

       250        260        270        280        290        300 
TVAWDLVGQA EHGYNSPVWL VTDSAALAEA VLAHIPGCIA DLPEPNRSSA QAAWDALGEV 

       310        320        330        340        350        360 
ILCTDREEMA ATADRYAPEH LHVQAADLDW WRGRLSAYGS LFLGELTTVA FGDKASGPNH 

       370        380        390        400        410        420 
VLPTSGAARY TGGLSVHKFL KTVTWQQVAP QALPDLARAT ATISRAEGME GHARTADIRL 

       430 
EKLRPTLRQV GTG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000031 Genomic DNA. Translation: AAV94285.1.
RefSeqYP_166233.1. NC_003911.12.

3D structure databases

ProteinModelPortalQ5LUS2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246200.SPO0981.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV94285; AAV94285; SPO0981.
GeneID3193830.
KEGGsil:SPO0981.
PATRIC23375249. VBIRuePom114501_0996.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK15509.
OMAIFIVADE.
OrthoDBEOG6CVVCR.

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 nameHISX2_RUEPO
AccessionPrimary (citable) accession number: Q5LUS2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: February 1, 2005
Last modified: May 14, 2014
This is version 71 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