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Q7U8K7 (HISX_SYNPX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. 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:SYNW0610
OrganismSynechococcus sp. (strain WH8102) [Complete proteome] [HAMAP]
Taxonomic identifier84588 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length437 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 – 437437Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135864

Sites

Active site3351Proton acceptor By similarity
Active site3361Proton acceptor By similarity
Metal binding2671Zinc By similarity
Metal binding2701Zinc By similarity
Metal binding3691Zinc By similarity
Metal binding4281Zinc By similarity
Binding site1371NAD By similarity
Binding site1991NAD By similarity
Binding site2221NAD By similarity
Binding site2451Substrate By similarity
Binding site2671Substrate By similarity
Binding site2701Substrate By similarity
Binding site3361Substrate By similarity
Binding site3691Substrate By similarity
Binding site4231Substrate By similarity
Binding site4281Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7U8K7 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 65B60CDC936925E7

FASTA43747,265
        10         20         30         40         50         60 
MSESRSLAFP LRCVRDRQQA EAELQRLTRR TQTSQQKDVQ GRVDVILKAV RERGDAAVCD 

        70         80         90        100        110        120 
FTERFDGFRP DPVAVPKHQL EQAWKALPEN LRDALELAHR RISEFHQRQR PEDIRMEGAH 

       130        140        150        160        170        180 
GEQLGRRWRP VQRAGLYVPG GRAAYPSTVL MNAVPARVAG VEQVVICSPA GSNGQVNPVV 

       190        200        210        220        230        240 
LAAAHLAGVH TVMRIGGAQA IAAMAFGTES VPKVDVISGP GNIYVTLAKQ AVYGQVGIDS 

       250        260        270        280        290        300 
LAGPSEVLVI ADQSAQPEQV AADLLAQAEH DPLASSVLIT TSHQLADGIS SAIAQQLEDH 

       310        320        330        340        350        360 
PRREICEASL RDWGLVVVCD DLETCAQLSD SFAPEHLELL VERPEALADR IQHAGAIFLG 

       370        380        390        400        410        420 
PWSPEAVGDY LAGPNHTLPT CAAARFSGAL SVETFMRHTS MIQFNRAALD ATASAVCELA 

       430 
ESEGLHSHAE SVRKRLS 

« Hide

References

[1]"The genome of a motile marine Synechococcus."
Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P., Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T., Dufresne A., Partensky F., Webb E.A., Waterbury J.
Nature 424:1037-1042(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WH8102.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX569690 Genomic DNA. Translation: CAE07125.1.
RefSeqNP_896703.1. NC_005070.1.

3D structure databases

ProteinModelPortalQ7U8K7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING84588.SYNW0610.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE07125; CAE07125; SYNW0610.
GeneID1732243.
KEGGsyw:SYNW0610.
PATRIC23832641. VBISynSp27240_0629.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.
ProtClustDBPRK00877.

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_SYNPX
AccessionPrimary (citable) accession number: Q7U8K7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 76 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