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Q5WIU9 (HISX1_BACSK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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 1

Short name=HDH 1
EC=1.1.1.23
Gene names
Name:hisD1
Ordered Locus Names:ABC1168
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length424 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 – 424424Histidinol dehydrogenase 1 HAMAP-Rule MF_01024
PRO_0000135724

Sites

Active site3181Proton acceptor By similarity
Active site3191Proton acceptor By similarity
Metal binding2501Zinc By similarity
Metal binding2531Zinc By similarity
Metal binding3521Zinc By similarity
Metal binding4111Zinc By similarity
Binding site1211NAD By similarity
Binding site1821NAD By similarity
Binding site2051NAD By similarity
Binding site2281Substrate By similarity
Binding site2501Substrate By similarity
Binding site2531Substrate By similarity
Binding site3191Substrate By similarity
Binding site3521Substrate By similarity
Binding site4061Substrate By similarity
Binding site4111Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WIU9 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 6131743AA063022E

FASTA42446,122
        10         20         30         40         50         60 
MAQYIKQGKS ESELKDSHGK VEQTVASLIA RIEKEGETAV RELSRQFDNW DPEQFRLSAE 

        70         80         90        100        110        120 
EIEKIVRSVP DQVKADICFA QEQIRHFAEQ QRASIQDIEV ETRPGVFLGH KNIPVNSVGC 

       130        140        150        160        170        180 
YIPGGRYPMV ASSHMSILTA KVAGVKRVIG CTPPINGEIP AATVTAMHFA GADEIYILGG 

       190        200        210        220        230        240 
VQAMTAMAVG TETIEAVDML VGPGNAFVAE AKRQLFGRVG IDLFAGPTEV LIIADDTADG 

       250        260        270        280        290        300 
EMVATDLLGQ AEHGPTSPAA LITTSKKLAE ETVAEIERQL QTLPTADVAK VAWEEHGMII 

       310        320        330        340        350        360 
LVDDLAEAVV EADKLAYEHV QVLTENPNYF LDHMTNYGAL FLGPETNVAY GDKVIGTNHT 

       370        380        390        400        410        420 
LPTKKAAKYT GGLWVGKFLK NCTYQRCTPE ASAEIGRIAE RLCELEGFIG HKAQASLRVK 


RYGK 

« 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: BAD63706.1.
RefSeqYP_174667.1. NC_006582.1.

3D structure databases

ProteinModelPortalQ5WIU9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING66692.ABC1168.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD63706; BAD63706; ABC1168.
GeneID3201041.
KEGGbcl:ABC1168.
PATRIC18921728. VBIBacCla58185_1252.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK15509.
OMAVPGGKYP.
OrthoDBEOG6CVVCR.
ProtClustDBPRK12447.

Enzyme and pathway databases

BioCycBCLA66692:GHMP-1214-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 nameHISX1_BACSK
AccessionPrimary (citable) accession number: Q5WIU9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: November 23, 2004
Last modified: February 19, 2014
This is version 69 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