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Q8ESR8 (HISX_OCEIH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. 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:OB0551
OrganismOceanobacillus iheyensis (strain DSM 14371 / JCM 11309 / KCTC 3954 / HTE831) [Complete proteome] [HAMAP]
Taxonomic identifier221109 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeOceanobacillus

Protein attributes

Sequence length427 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 – 427427Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135807

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
Q8ESR8 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 62E9843506AC5F47

FASTA42746,545
        10         20         30         40         50         60 
MEILSLHQWK QQQDTKSSTI RNKQVDQDVL RIIEQVQIQG DEALKHYTLQ FDQVNLNSFE 

        70         80         90        100        110        120 
VTSNEWEQAI KKVDSTLLDA LETAAGNIQR YQSEMLESNW SITPETGVKL GQQVNPLDRV 

       130        140        150        160        170        180 
GIYIPGGKAS YPSTVLMDAI PAKVAGVKEI IITSPPNKNG EIDPVVLAAA KIAGVTKVYK 

       190        200        210        220        230        240 
VGGAQAIAAL TYGTETIPSV DKIVGPGNIY VTRAKKWVFG DIAIDMIAGP SEICIFADSS 

       250        260        270        280        290        300 
APVPYVAADL LSQAEHDEEA SSLCITTDRS FAKLLQEEVN RQIPLLERKE IIEASISQNG 

       310        320        330        340        350        360 
KIIICDNNEE AINTINQLAP EHLQLMTIDS EQLCPKIKHA GAIFIGNYSS EPLGDYFAGP 

       370        380        390        400        410        420 
SHTLPTNGTA KFSSPLGVYD FVKKTSLIQY SKNKLAEAAD TIITLAEAEG LTAHANAIRI 


RKENDNA 

« Hide

References

[1]"Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments."
Takami H., Takaki Y., Uchiyama I.
Nucleic Acids Res. 30:3927-3935(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14371 / JCM 11309 / KCTC 3954 / HTE831.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000028 Genomic DNA. Translation: BAC12507.1.
RefSeqNP_691472.1. NC_004193.1.

3D structure databases

ProteinModelPortalQ8ESR8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING221109.OB0551.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC12507; BAC12507; BAC12507.
GeneID1015849.
KEGGoih:OB0551.
PATRIC22792025. VBIOceIhe82024_0565.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycOIHE221109:GI2A-596-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_OCEIH
AccessionPrimary (citable) accession number: Q8ESR8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 83 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