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Q5WDH8 (HISX2_BACSK) 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:ABC3048
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length425 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 – 425425Histidinol dehydrogenase 2 HAMAP-Rule MF_01024
PRO_0000135725

Sites

Active site3211Proton acceptor By similarity
Active site3221Proton acceptor By similarity
Metal binding2531Zinc By similarity
Metal binding2561Zinc By similarity
Metal binding3551Zinc By similarity
Metal binding4141Zinc By similarity
Binding site1231NAD By similarity
Binding site1851NAD By similarity
Binding site2081NAD By similarity
Binding site2311Substrate By similarity
Binding site2531Substrate By similarity
Binding site2561Substrate By similarity
Binding site3221Substrate By similarity
Binding site3551Substrate By similarity
Binding site4091Substrate By similarity
Binding site4141Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WDH8 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 071216AAFCD82413

FASTA42544,989
        10         20         30         40         50         60 
MKIIELKEGE AVSLKRSGLH GSEAEIATVN TIIETVKKEG DQALVDYTQQ FDGVELTDLC 

        70         80         90        100        110        120 
VTKAELDNAY RHIDQPVLAA IRQAIANVRA FHEQQKAKSW FQTAPDGTIL GQRVTPLDAV 

       130        140        150        160        170        180 
GVYVPGGKAA YPSSIIMNVV PAQVAGVKDI SMVSPSGKNG TLPPAVLATA AELGVHTIYK 

       190        200        210        220        230        240 
LGGAQAVAAL AYGTETVRPV DKITGPGNKY VALAKRAVFG DVAIDMIAGP SEICVLADEK 

       250        260        270        280        290        300 
ANPAYVAADL LSQAEHDEDA TAVLVTPSRK LAEAVQQETA RQLATLPRKE IAGRALEQFG 

       310        320        330        340        350        360 
ALYVTASLAQ AIEVVNQLAP EHLEIATEEP LALLGRVKHA GAIFLGSYSA EPVGDYFAGP 

       370        380        390        400        410        420 
NHVLPTNGTA RFASPLSVDD FVKKSSIISY SKTALAENGK AITELARLEG LEAHARAIDI 


RLEDM 

« Hide

References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KSM-K16.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006627 Genomic DNA. Translation: BAD65582.1.
RefSeqYP_176543.1. NC_006582.1.

3D structure databases

ProteinModelPortalQ5WDH8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING66692.ABC3048.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD65582; BAD65582; ABC3048.
GeneID3204579.
KEGGbcl:ABC3048.
PATRIC18925810. VBIBacCla58185_3254.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAYAAKLCG.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycBCLA66692:GHMP-3130-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 nameHISX2_BACSK
AccessionPrimary (citable) accession number: Q5WDH8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: November 23, 2004
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