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UniProtKB/Swiss-Prot entry Q8FNZ0

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

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Entry information
Entry name HISX_COREF
Primary accession number Q8FNZ0
Secondary accession numbers None
Integrated into Swiss-Prot on March 25, 2003
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 42)
Name and origin of the protein
Protein name Histidinol dehydrogenase
Synonyms HDH
EC 1.1.1.23
Gene name
Name: hisD
OrderedLocusNames: CE2003
From
Corynebacterium efficiens [TaxID: 152794] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Corynebacteriaceae; Corynebacterium.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
DOI=10.1101/gr.1285603; PubMed=12840036 [NCBI, ExPASy, EBI, Israel, Japan]
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens.";
Genome Res. 13:1572-1579(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
BA000035; BAC18813.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_738613.1; -.
3D structure databases
HSSP P06988; 1K75. [HSSP ENTRY / PDB]
ModBase Q8FNZ0.
Enzyme and pathway databases
BioCyc CEFF196164:CE2003-MON; -.
Ontologies
GO
GO:0004399; Molecular function: histidinol dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
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.
Genome annotation databases
GeneID 1032060; -.
GenomeReviews BA000035_GR; CE2003.
KEGG cef:CE2003; -.
NMPDR fig|196164.1.peg.2003; -.
Phylogenomic databases
HOGENOM Q8FNZ0; -.
Genome annotation databases
CMR Q8FNZ0; CE2003.
Other
ProtoNet Q8FNZ0.
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   451  451     Histidinol dehydrogenase. PRO_0000135760
ACT_SITE   332   332        Proton acceptor (By similarity). 
ACT_SITE   333   333        Proton acceptor (By similarity). 
METAL   263   263        Zinc (By similarity). 
METAL   266   266        Zinc (By similarity). 
METAL   366   366        Zinc (By similarity). 
METAL   425   425        Zinc (By similarity). 
BINDING   129   129        NAD (By similarity). 
BINDING   193   193        NAD (By similarity). 
BINDING   218   218        NAD (By similarity). 
BINDING   241   241        Substrate (By similarity). 
BINDING   263   263        Substrate (By similarity). 
BINDING   266   266        Substrate (By similarity). 
BINDING   333   333        Substrate (By similarity). 
BINDING   366   366        Substrate (By similarity). 
BINDING   420   420        Substrate (By similarity). 
BINDING   425   425        Substrate (By similarity). 
Sequence information
Length: 451 AA [This is the length of the unprocessed precursor] Molecular weight: 47770 Da [This is the MW of the unprocessed precursor] CRC64: 5A2D5AA7B990ECCF [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLNVTDLRGH TPSKSDIRRA LPRGGTDVVS VLPIVEPVVD DVQNRGAEAA LDYGEKFDHI 

        70         80         90        100        110        120 
RPASVRVPAE VLKAAEDTLD PRVREAIEES IRRVRKVHAD QKPREHTTEL APGGTVTERF 

       130        140        150        160        170        180 
LPIDRVGLYV PGGNAVYPSS VIMNAVPAQE AGVGTLVVAS PPQADHGGWP HPTILAACSI 

       190        200        210        220        230        240 
LGVDEVWAVG GAQAVALLAF GDDSADLEPV DIITGPGNIF VTAAKRLVRG VVGTDSEAGP 

       250        260        270        280        290        300 
TEIAILADDT ANPVNVAYDL ISQAEHDVMA ASVLITDSEQ LARDVNREIE ARYAITRNAD 

       310        320        330        340        350        360 
RVAEALRGKQ SGIVLVDDIE VGIAVADQYA AEHLEVHTAN AREVSERISN AGAIFVGDFS 

       370        380        390        400        410        420 
PVPLGDYSAG SNHVLPTSGT ARFSAGLSTH TFLRPVNLIE YDEAALKDIS EVVINFADAE 

       430        440        450 
DLPAHGEAIR ARFETLPTTT ADTTDTPDAT A
Q8FNZ0 in FASTA format

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