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Q8FNZ0 (HISX_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 82. 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:CE2003
OrganismCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) [Complete proteome] [HAMAP]
Taxonomic identifier196164 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length451 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 – 451451Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135760

Sites

Active site3321Proton acceptor By similarity
Active site3331Proton acceptor By similarity
Metal binding2631Zinc By similarity
Metal binding2661Zinc By similarity
Metal binding3661Zinc By similarity
Metal binding4251Zinc By similarity
Binding site1291NAD By similarity
Binding site1931NAD By similarity
Binding site2181NAD By similarity
Binding site2411Substrate By similarity
Binding site2631Substrate By similarity
Binding site2661Substrate By similarity
Binding site3331Substrate By similarity
Binding site3661Substrate By similarity
Binding site4201Substrate By similarity
Binding site4251Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FNZ0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 5A2D5AA7B990ECCF

FASTA45147,770
        10         20         30         40         50         60 
MLNVTDLRGH TPSKSDIRRA LPRGGTDVVS VLPIVEPVVD DVQNRGAEAA LDYGEKFDHI 

        70         80         90        100        110        120 
RPASVRVPAE VLKAAEDTLD PRVREAIEES IRRVRKVHAD QKPREHTTEL APGGTVTERF 

       130        140        150        160        170        180 
LPIDRVGLYV PGGNAVYPSS VIMNAVPAQE AGVGTLVVAS PPQADHGGWP HPTILAACSI 

       190        200        210        220        230        240 
LGVDEVWAVG GAQAVALLAF GDDSADLEPV DIITGPGNIF VTAAKRLVRG VVGTDSEAGP 

       250        260        270        280        290        300 
TEIAILADDT ANPVNVAYDL ISQAEHDVMA ASVLITDSEQ LARDVNREIE ARYAITRNAD 

       310        320        330        340        350        360 
RVAEALRGKQ SGIVLVDDIE VGIAVADQYA AEHLEVHTAN AREVSERISN AGAIFVGDFS 

       370        380        390        400        410        420 
PVPLGDYSAG SNHVLPTSGT ARFSAGLSTH TFLRPVNLIE YDEAALKDIS EVVINFADAE 

       430        440        450 
DLPAHGEAIR ARFETLPTTT ADTTDTPDAT A 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC18813.1.
RefSeqNP_738613.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8FNZ0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196164.CE2003.

Proteomic databases

PRIDEQ8FNZ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC18813; BAC18813; BAC18813.
GeneID1032060.
KEGGcef:CE2003.
PATRIC21490139. VBICorEff9312_1984.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.
ProtClustDBPRK00877.

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_COREF
AccessionPrimary (citable) accession number: Q8FNZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 82 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