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Q7VQX0 (HISX_BLOFL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Histidinol dehydrogenase
Short name=HDH
EC=1.1.1.23
Gene names
Name:hisD
Ordered Locus Names:Bfl463
OrganismBlochmannia floridanus [Complete proteome] [HAMAP]
Taxonomic identifier203907 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › ant endosymbionts › Candidatus Blochmannia

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.

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP-Rule MF_01024

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the histidinol dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135734

Sites

Active site3291Proton acceptor By similarity
Active site3301Proton acceptor By similarity
Metal binding2621Zinc By similarity
Metal binding2651Zinc By similarity
Metal binding3631Zinc By similarity
Metal binding4221Zinc By similarity
Binding site1331NAD By similarity
Binding site1911NAD By similarity
Binding site2141NAD By similarity
Binding site2401Substrate By similarity
Binding site2621Substrate By similarity
Binding site2651Substrate By similarity
Binding site3301Substrate By similarity
Binding site3631Substrate By similarity
Binding site4171Substrate By similarity
Binding site4221Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VQX0 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: C49F52E83233E46E

FASTA43748,711
        10         20         30         40         50         60 
MISTQYLIPT YWHRCSISEQ LTLLTRPINK HNNSIHLDVK YILDHVSKLG DNALIKFNLQ 

        70         80         90        100        110        120 
FDYVNTISLK ISPNKIINSG NSLSKPIKKA IHSAIDNITR FHTAQYFPKV DLEIIPGVRC 

       130        140        150        160        170        180 
KQIIRPLHTI GLYVPGGSTP LPSTVMMLGI PAKIAQCKRI ILCSPPPIPN IILYTAQLCG 

       190        200        210        220        230        240 
IEEIYQVGGA QAIAAMGFGT ESIPRVDKIF GPGNIWVTEA KRQIHYITNK VAIDMLAGPS 

       250        260        270        280        290        300 
EILIIADKTA NPIFIAADLL SQAEHGPDSH IILITPDMNL AQQTRQELYK QIQNLDRIDI 

       310        320        330        340        350        360 
IHQSLTHARI IITDNIMECF QISNDYAPEH LLIQTQNPEN YLKYITNAGS IFLGHWSPES 

       370        380        390        400        410        420 
AGDYASGTNH VLPTYGHATT TSALGVADFQ KRILVQELTQ HGLLQLSSTI QTLTKIEKLK 

       430 
AHEYSVIHRI NYIKGTT

« Hide

References

[1]"The genome sequence of Blochmannia floridanus: comparative analysis of reduced genomes."
Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F., Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B., van Ham R.C.H.J., Gross R., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX248583 Genomic DNA. Translation: CAD83522.1.
RefSeqNP_878746.1. NC_005061.1.

3D structure databases

ProteinModelPortalQ7VQX0.
SMRQ7VQX0. Positions 10-435.
ModBaseSearch...

Protein-protein interaction databases

STRING203907.Bfl463.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD83522; CAD83522; Bfl463.
GeneID1499663.
KEGGbfl:Bfl463.
PATRIC31964537. VBICanBlo38691_0451.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPTYGYSR.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycBFLO203907:GHF7-478-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. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHISX_BLOFL
AccessionPrimary (citable) accession number: Q7VQX0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2003
Last modified: May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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