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UniProtKB/Swiss-Prot entry Q7VQX0

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HISX_BLOFL
Primary accession number Q7VQX0
Secondary accession numbers None
Integrated into Swiss-Prot on April 13, 2004
Sequence was last modified on October 1, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 36)
Name and origin of the protein
Protein name Histidinol dehydrogenase
Synonyms HDH
EC 1.1.1.23
Gene name
Name: hisD
OrderedLocusNames: Bfl463
From
Blochmannia floridanus [TaxID: 203907] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.1533499100; PubMed=12886019 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Blochmannia floridanus: comparative analysis of reduced genomes.";
Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
BX248583; CAD83522.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_878746.1; -.
3D structure databases
ModBase Q7VQX0.
Enzyme and pathway databases
BioCyc CBLO203907:BFL463-MON; -.
Ontologies
GO
GO:0004399; Molecular function: histidinol dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0000105; Biological process: histidine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01024; -; 1.
PBIL [Tree]
InterPro IPR001692; Histidinol_DHase.
IPR012131; Hstdl_DHase_prok.
Graphical view of domain structure.
PANTHER PTHR21256:SF2; Hstdl_DH_prok; 1.
Pfam PF00815; Histidinol_dh; 1.
Pfam graphical view of domain structure.
PRINTS PR00083; HOLDHDRGNASE.
ProDom PD002680; Histidinol_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00069; hisD; 1.
PROSITE PS00611; HISOL_DEHYDROGENASE; 1.
BLOCKS Q7VQX0.
Genome annotation databases
GeneID 1499663; -.
GenomeReviews BX248583_GR; Bfl463.
KEGG bfl:Bfl463; -.
Phylogenomic databases
HOGENOM Q7VQX0; -.
Genome annotation databases
CMR Q7VQX0; Bfl463.
Other
ProtoNet Q7VQX0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; Metal-binding; NAD; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   437  437     Histidinol dehydrogenase. PRO_0000135734
ACT_SITE   329   329        Proton acceptor (By similarity). 
ACT_SITE   330   330        Proton acceptor (By similarity). 
METAL   262   262        Zinc (By similarity). 
METAL   265   265        Zinc (By similarity). 
METAL   363   363        Zinc (By similarity). 
METAL   422   422        Zinc (By similarity). 
BINDING   133   133        NAD (By similarity). 
BINDING   191   191        NAD (By similarity). 
BINDING   214   214        NAD (By similarity). 
BINDING   240   240        Substrate (By similarity). 
BINDING   262   262        Substrate (By similarity). 
BINDING   265   265        Substrate (By similarity). 
BINDING   330   330        Substrate (By similarity). 
BINDING   363   363        Substrate (By similarity). 
BINDING   417   417        Substrate (By similarity). 
BINDING   422   422        Substrate (By similarity). 
Sequence information
Length: 437 AA [This is the length of the unprocessed precursor] Molecular weight: 48711 Da [This is the MW of the unprocessed precursor] CRC64: C49F52E83233E46E [This is a checksum on the sequence] 
        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
Q7VQX0 in FASTA format

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