Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P60858 (HISX_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 80. 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:DIP1566
OrganismCorynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) [Complete proteome] [HAMAP]
Taxonomic identifier257309 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length449 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 – 449449Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135759

Sites

Active site3431Proton acceptor By similarity
Active site3441Proton acceptor By similarity
Metal binding2741Zinc By similarity
Metal binding2771Zinc By similarity
Metal binding3771Zinc By similarity
Metal binding4361Zinc By similarity
Binding site1351NAD By similarity
Binding site1991NAD By similarity
Binding site2291NAD By similarity
Binding site2521Substrate By similarity
Binding site2741Substrate By similarity
Binding site2771Substrate By similarity
Binding site3441Substrate By similarity
Binding site3771Substrate By similarity
Binding site4311Substrate By similarity
Binding site4361Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P60858 [UniParc].

Last modified April 13, 2004. Version 1.
Checksum: 002BB36B98F433FB

FASTA44947,762
        10         20         30         40         50         60 
MRKRKIMLNV IDLRGHVPTT SELRRTLPRG GTDINSVLPI VEPVVTDVKN RGAAAALDYG 

        70         80         90        100        110        120 
EKFDHVRPTS IRVPQDVIDQ ALDSLDPNVI EALKESIARV RAVHSEQLPA QHTTSFGEGA 

       130        140        150        160        170        180 
TITEKFIPVS RVGLYAPGGN AVYPSSVIMN VVPAQEAGVE SLVVASPPQK DHGGWPHPTI 

       190        200        210        220        230        240 
LAAAKLLGVT EVWAMGGAQA VALLAYGDDT QQNSAEVLEP VDMITGPGNI FVTAAKRLVR 

       250        260        270        280        290        300 
GVVGIDSEAG PTEIAIVADA QANPVWIAYD LISQAEHDVL AASVLITDSE ELAQRVNEEV 

       310        320        330        340        350        360 
AARYSVTRNA DRVSEALKGQ QSGIVLVDDL PTAVIVADAY AAEHLEIHTA ESHKVAEQIR 

       370        380        390        400        410        420 
NAGAIFVGGY SPVPLGDYSA GSNHVLPTSG SARYSSGLST HTFLKPVNVI YYDEVALKEI 

       430        440 
SDTVITLADA EDLPAHGEAI RTRFENLGN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248358 Genomic DNA. Translation: CAE50091.1.
RefSeqNP_939908.1. NC_002935.2.

3D structure databases

ProteinModelPortalP60858.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257309.DIP1566.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE50091; CAE50091; DIP1566.
GeneID2650755.
KEGGcdi:DIP1566.
PATRIC21484340. VBICorDip47633_1546.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAHTERITQ.
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 nameHISX_CORDI
AccessionPrimary (citable) accession number: P60858
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: May 14, 2014
This is version 80 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