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UniProtKB/Swiss-Prot entry P62456

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

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Entry information
Entry name HISX_BACC1
Primary accession number P62456
Secondary accession numbers None
Integrated into Swiss-Prot on July 5, 2004
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 38)
Name and origin of the protein
Protein name Histidinol dehydrogenase
Synonyms HDH
EC 1.1.1.23
Gene name
Name: hisD
OrderedLocusNames: BCE_1526
From
Bacillus cereus (strain ATCC 10987) [TaxID: 222523] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus group.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/nar/gkh258; PubMed=14960714 [NCBI, ExPASy, EBI, Israel, Japan]
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1.";
Nucleic Acids Res. 32:977-988(2004).
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
AE017194; AAS40455.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_977847.1; -.
3D structure databases
ModBase P62456.
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).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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 P62456.
ProtoNet P62456.
Genome annotation databases
GeneID 2748395; -.
GenomeReviews AE017194_GR; BCE_1526.
KEGG bca:BCE_1526; -.
NMPDR fig|222523.1.peg.1519; -.
TIGR BCE_1526; -.
Phylogenomic databases
HOGENOM P62456; -.
Other
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   429  429     Histidinol dehydrogenase. PRO_0000135721
ACT_SITE   324   324        Proton acceptor (By similarity). 
ACT_SITE   325   325        Proton acceptor (By similarity). 
METAL   256   256        Zinc (By similarity). 
METAL   259   259        Zinc (By similarity). 
METAL   358   358        Zinc (By similarity). 
METAL   417   417        Zinc (By similarity). 
BINDING   127   127        NAD (By similarity). 
BINDING   188   188        NAD (By similarity). 
BINDING   211   211        NAD (By similarity). 
BINDING   234   234        Substrate (By similarity). 
BINDING   256   256        Substrate (By similarity). 
BINDING   259   259        Substrate (By similarity). 
BINDING   325   325        Substrate (By similarity). 
BINDING   358   358        Substrate (By similarity). 
BINDING   412   412        Substrate (By similarity). 
BINDING   417   417        Substrate (By similarity). 
Sequence information
Length: 429 AA [This is the length of the unprocessed precursor] Molecular weight: 47360 Da [This is the MW of the unprocessed precursor] CRC64: FBA64A1F6C18A30A [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MEIVFEDFQK ALSKIKLLRE NANIIEETVQ RNVSEIVRNV RESGDEALSF YTKKFDGVKI 

        70         80         90        100        110        120 
KEFRVSEEEE KRASMFVENS FLEALQEAKK NIISYHEKQK RQSMFDCASE GIIRGQIIRP 

       130        140        150        160        170        180 
LENVGVYVPG GTASYPSSVL MNVLPAKLAG VKKIVMVTPP REGGIDPHIL VAASLAGVDE 

       190        200        210        220        230        240 
IYTIGGAQAI AALAYGTESI PKVDKIVGPG NLYVALAKRE VYGIVNIDMI AGPSEIVVIA 

       250        260        270        280        290        300 
DETGNAKYIA ADLLSQAEHD ERATAICITT NIELAKKVEK EIERQLETLP RSEIARESIN 

       310        320        330        340        350        360 
RNGAIFIVPS IDEALQLSNE IAPEHLELHI KEPMNALAYV KHAGSIFLGP YAPEPLGDYL 

       370        380        390        400        410        420 
AGPNHVLPTS GTARFFSPLS VDDFVKKSSF LSYTEEALRD VQHHIVELAN KEGLHAHARA 


IQIRFEEEE
P62456 in FASTA format

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