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Q5E638 (HISX_VIBF1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. 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:VF_1013
OrganismVibrio fischeri (strain ATCC 700601 / ES114) [Reference proteome] [HAMAP]
Taxonomic identifier312309 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length439 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
Reference 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 – 439439Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135875

Sites

Active site3231Proton acceptor By similarity
Active site3241Proton acceptor By similarity
Metal binding2561Zinc By similarity
Metal binding2591Zinc By similarity
Metal binding3571Zinc By similarity
Metal binding4161Zinc By similarity
Binding site1271NAD By similarity
Binding site1851NAD By similarity
Binding site2081NAD By similarity
Binding site2341Substrate By similarity
Binding site2561Substrate By similarity
Binding site2591Substrate By similarity
Binding site3241Substrate By similarity
Binding site3571Substrate By similarity
Binding site4111Substrate By similarity
Binding site4161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5E638 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 83ABB202021C0078

FASTA43946,846
        10         20         30         40         50         60 
MKTLVWQSLS DSQQDTVLQR PAITEGANIT AAVTSVINTV KQEGDAGVFA LTEKFDGVKP 

        70         80         90        100        110        120 
DSIRVSNAEI EAASDRLSEE MKTALKQAYS NISKFHQAQK PQPVKVETQP GVICEQITMP 

       130        140        150        160        170        180 
INKVGLYIPG GSAPLPSTVL MLGIPAQIAG CHKVVLCSPP PIADEILYVA KLCKIDEVYN 

       190        200        210        220        230        240 
IGGAQAVAAM AYGTESVSKV DKIFGPGNAY VTEAKRQVSN DFRGAAIDMP AGPSEVLVIA 

       250        260        270        280        290        300 
DESADPDFIA ADLLSQAEHG PDSQVVLVTP SPIIADQVAD AVERQLKELS REDIARQALG 

       310        320        330        340        350        360 
SSLLIVADSL TQCVSISNFY GPEHLIVQTK NPRELLPLLD NAGSIFLGDY SPESAGDYAS 

       370        380        390        400        410        420 
GTNHVLPTYG YTRTYSSLGL ADFSKRMTVQ ELTADGLKGL APTVVTMAEA EGLDAHKRAV 

       430 
TIRIEKLAQL DVNKQEVNQ 

« Hide

References

[1]"Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with pathogenic congeners."
Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., Stevens A., Visick K., Whistler C., Greenberg E.P.
Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700601 / ES114.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000020 Genomic DNA. Translation: AAW85508.1.
RefSeqYP_204396.1. NC_006840.2.

3D structure databases

ProteinModelPortalQ5E638.
SMRQ5E638. Positions 6-429.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING312309.VF_1013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW85508; AAW85508; VF_1013.
GeneID3277807.
KEGGvfi:VF_1013.
PATRIC20112620. VBIVibFis127983_1013.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycAFIS312309:GIWP-1069-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_VIBF1
AccessionPrimary (citable) accession number: Q5E638
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: March 15, 2005
Last modified: February 19, 2014
This is version 68 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