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Q5YYQ0 (HISX_NOCFA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. 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:NFA_18450
OrganismNocardia farcinica (strain IFM 10152) [Complete proteome] [HAMAP]
Taxonomic identifier247156 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeNocardia

Protein attributes

Sequence length445 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 – 445445Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135806

Sites

Active site3401Proton acceptor By similarity
Active site3411Proton acceptor By similarity
Metal binding2711Zinc By similarity
Metal binding2741Zinc By similarity
Metal binding3741Zinc By similarity
Metal binding4331Zinc By similarity
Binding site1341NAD By similarity
Binding site1981NAD By similarity
Binding site2261NAD By similarity
Binding site2491Substrate By similarity
Binding site2711Substrate By similarity
Binding site2741Substrate By similarity
Binding site3411Substrate By similarity
Binding site3741Substrate By similarity
Binding site4281Substrate By similarity
Binding site4331Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5YYQ0 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 90C2C883B64D9081

FASTA44545,665
        10         20         30         40         50         60 
MTSRIELARV DLRGRTPSTA ELRAALPRGG VDVDSVLHHV RPVVEAVRER GAAAALEFGE 

        70         80         90        100        110        120 
KFDGVVPATV RVPAAELARA LDELDPAVRA ALEESIARAR RVHADQRRTD TTTEVVPGGT 

       130        140        150        160        170        180 
VTERWVPVAR VGLYVPGGNA VYPSSVVMNV VPAQTAGVGS LVVASPPQAN FGGLPHPTIL 

       190        200        210        220        230        240 
AAAALLGVEE VWAVGGAQAV ALLSYGGTDT DGAPLDPVDL ITGPGNIYVT AAKRLCRGLV 

       250        260        270        280        290        300 
GIDAEAGPTE IAILADATAD PAHVAADLIS QAEHDVLAAS VLVTDSVALA DAVDAALTAQ 

       310        320        330        340        350        360 
LAVVKHAERV RTALTGKQSG TVLVDDITQG LRVVDAYAAE HLEIQTADAS AVAARVRSAG 

       370        380        390        400        410        420 
AVFVGPYAPV SLGDYCAGSN HVLPTAGCAR HSSGLSVQTF LRGIHVVEYT EAALKDVAGH 

       430        440 
VVALADAEDL PAHGQAVTVR FEALS 

« Hide

References

[1]"The complete genomic sequence of Nocardia farcinica IFM 10152."
Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K., Shiba T., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IFM 10152.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006618 Genomic DNA. Translation: BAD56691.1.
RefSeqYP_118055.1. NC_006361.1.

3D structure databases

ProteinModelPortalQ5YYQ0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING247156.nfa18450.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD56691; BAD56691; NFA_18450.
GeneID3109568.
KEGGnfa:nfa18450.
PATRIC22733308. VBINocFar94200_1896.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
KOK00013.
OMADEMAMPI.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycNFAR247156:GJ9T-1886-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_NOCFA
AccessionPrimary (citable) accession number: Q5YYQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 74 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