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UniProtKB/Swiss-Prot entry Q6FEC8

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

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Entry information
Entry name HISX_ACIAD
Primary accession number Q6FEC8
Secondary accession numbers None
Integrated into Swiss-Prot on December 7, 2004
Sequence was last modified on July 19, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 32)
Name and origin of the protein
Protein name Histidinol dehydrogenase
Synonyms HDH
EC 1.1.1.23
Gene name
Name: hisD
OrderedLocusNames: ACIAD0663
From
Acinetobacter sp. (strain ADP1) [TaxID: 62977] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Acinetobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/nar/gkh910; PubMed=15514110 [NCBI, ExPASy, EBI, Israel, Japan]
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium.";
Nucleic Acids Res. 32:5766-5779(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
CR543861; CAG67580.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_045402.1; -.
3D structure databases
ModBase Q6FEC8.
Enzyme and pathway databases
BioCyc ASP62977:ACIAD0663-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 Q6FEC8.
Genome annotation databases
GeneID 2878926; -.
GenomeReviews CR543861_GR; ACIAD0663.
KEGG aci:ACIAD0663; -.
NMPDR fig|62977.3.peg.361; -.
Phylogenomic databases
HOGENOM Q6FEC8; -.
Genome annotation databases
CMR Q6FEC8; ACIAD0663.
Other
ProtoNet Q6FEC8.
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   430  430     Histidinol dehydrogenase. PRO_0000135713
ACT_SITE   328   328        Proton acceptor (By similarity). 
ACT_SITE   329   329        Proton acceptor (By similarity). 
METAL   260   260        Zinc (By similarity). 
METAL   263   263        Zinc (By similarity). 
METAL   362   362        Zinc (By similarity). 
METAL   421   421        Zinc (By similarity). 
BINDING   131   131        NAD (By similarity). 
BINDING   192   192        NAD (By similarity). 
BINDING   215   215        NAD (By similarity). 
BINDING   238   238        Substrate (By similarity). 
BINDING   260   260        Substrate (By similarity). 
BINDING   263   263        Substrate (By similarity). 
BINDING   329   329        Substrate (By similarity). 
BINDING   362   362        Substrate (By similarity). 
BINDING   416   416        Substrate (By similarity). 
BINDING   421   421        Substrate (By similarity). 
Sequence information
Length: 430 AA [This is the length of the unprocessed precursor] Molecular weight: 46671 Da [This is the MW of the unprocessed precursor] CRC64: 75B7CFF03AB94510 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MMRRLSTQDQ SFKQVFADLL AFETVNDPEL LKTVDQIIAD VRQYGDEHVL KLTQQFDRHP 

        70         80         90        100        110        120 
AHQFSDLELT QEQLKTAFEA LTAEIREALE LAAERIRSFH QAQKQEGWSY VDALGNTLGQ 

       130        140        150        160        170        180 
KVTPLDRVGI YVPGGLASYP SSVLMNAIPA HVAGVPEIIM VVPAPNGELN SLVLAAAYLA 

       190        200        210        220        230        240 
GVSRIFTIGG AQAVAALAYG TQTIPAVDKI TGPGNRFVAA AKRAVFGQVG IDMIAGPSEI 

       250        260        270        280        290        300 
LVYAEGQNNA KWLAMDLLSQ AEHDTVAQAI FITPDEALLD EVAQAIEEHL AALPKADIAR 

       310        320        330        340        350        360 
TSIANRGALV LVKDRDEAIE LINQVAPEHL ELCLDESEAM SQKIRHAGAI FMGRYTPEAI 

       370        380        390        400        410        420 
GDYCAGPNHV LPTSGTARFS SPLGVYDFQK RSSLIMCSQE GVKSLAKAAD VLAQQENLDA 

       430 
HARSARYRYQ
Q6FEC8 in FASTA format

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