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Q9L6I1 (HISX_THIRO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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
OrganismThiocapsa roseopersicina
Taxonomic identifier1058 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeThiocapsa

Protein attributes

Sequence length233 AA.
Sequence statusFragment.
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.

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.

Sequence similarities

Belongs to the histidinol dehydrogenase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 233›233Histidinol dehydrogenase
PRO_0000135873

Sites

Active site1211Proton acceptor By similarity
Active site1221Proton acceptor By similarity
Metal binding531Zinc By similarity
Metal binding561Zinc By similarity
Metal binding1551Zinc By similarity
Metal binding2141Zinc By similarity
Binding site311Substrate By similarity
Binding site531Substrate By similarity
Binding site561Substrate By similarity
Binding site1221Substrate By similarity
Binding site1551Substrate By similarity
Binding site2091Substrate By similarity
Binding site2141Substrate By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q9L6I1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: EDF15B51B24D45F0

FASTA23324,671
        10         20         30         40         50         60 
DKIVGPGNIY VATAKRAVFG QVGIDMVAGP SEILVVCDGA TDPDWIAMDL FSQAEHDEDA 

        70         80         90        100        110        120 
QSILLSWDAD FLDRVAASIE RLLPSMERET IIATALRGRG AMILARDLDD AIAVANRIAP 

       130        140        150        160        170        180 
EHLELSVEDP QAIVGRIRHA GAIFMGRYTA EAIGDYCAGP NHVLPTSRTA RFSSPLGVYD 

       190        200        210        220        230 
FQKRSSLIMA SAAGAAQLAK TASVLARGEG LTAHARSAEY RGAVEPAAEP GLS 

« Hide

References

[1]"Genes for putative enzymes of histidine biosynthesis from the phototrophic sulfur bacterium Thiocapsa roseopersicina."
Milles J., Kappler U., Truper H.G., Dahl C.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF235018 Genomic DNA. Translation: AAF44661.1.

3D structure databases

ProteinModelPortalQ9L6I1.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00031; UER00014.

Family and domain databases

InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR012131. Hstdl_DH.
[Graphical view]
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHISX_THIRO
AccessionPrimary (citable) accession number: Q9L6I1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 63 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