ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q5WIU9


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name HISX1_BACSK
Primary accession number Q5WIU9
Secondary accession numbers None
Integrated into Swiss-Prot on January 10, 2006
Sequence was last modified on November 23, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 28)
Name and origin of the protein
Protein name Histidinol dehydrogenase 1
Synonyms HDH 1
EC 1.1.1.23
Gene name
Name: hisD1
OrderedLocusNames: ABC1168
From
Bacillus clausii (strain KSM-K16) [TaxID: 66692] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.;
"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16.";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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
AP006627; BAD63706.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_174667.1; -.
3D structure databases
ModBase Q5WIU9.
Enzyme and pathway databases
BioCyc BCLA66692:ABC1168-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 Q5WIU9.
Genome annotation databases
GeneID 3201041; -.
GenomeReviews AP006627_GR; ABC1168.
KEGG bcl:ABC1168; -.
NMPDR fig|66692.3.peg.742; -.
Phylogenomic databases
HOGENOM Q5WIU9; -.
Genome annotation databases
CMR Q5WIU9; ABC1168.
Other
ProtoNet Q5WIU9.
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   424  424     Histidinol dehydrogenase 1. PRO_0000135724
ACT_SITE   318   318        Proton acceptor (By similarity). 
ACT_SITE   319   319        Proton acceptor (By similarity). 
METAL   250   250        Zinc (By similarity). 
METAL   253   253        Zinc (By similarity). 
METAL   352   352        Zinc (By similarity). 
METAL   411   411        Zinc (By similarity). 
BINDING   121   121        NAD (By similarity). 
BINDING   182   182        NAD (By similarity). 
BINDING   205   205        NAD (By similarity). 
BINDING   228   228        Substrate (By similarity). 
BINDING   250   250        Substrate (By similarity). 
BINDING   253   253        Substrate (By similarity). 
BINDING   319   319        Substrate (By similarity). 
BINDING   352   352        Substrate (By similarity). 
BINDING   406   406        Substrate (By similarity). 
BINDING   411   411        Substrate (By similarity). 
Sequence information
Length: 424 AA [This is the length of the unprocessed precursor] Molecular weight: 46122 Da [This is the MW of the unprocessed precursor] CRC64: 6131743AA063022E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAQYIKQGKS ESELKDSHGK VEQTVASLIA RIEKEGETAV RELSRQFDNW DPEQFRLSAE 

        70         80         90        100        110        120 
EIEKIVRSVP DQVKADICFA QEQIRHFAEQ QRASIQDIEV ETRPGVFLGH KNIPVNSVGC 

       130        140        150        160        170        180 
YIPGGRYPMV ASSHMSILTA KVAGVKRVIG CTPPINGEIP AATVTAMHFA GADEIYILGG 

       190        200        210        220        230        240 
VQAMTAMAVG TETIEAVDML VGPGNAFVAE AKRQLFGRVG IDLFAGPTEV LIIADDTADG 

       250        260        270        280        290        300 
EMVATDLLGQ AEHGPTSPAA LITTSKKLAE ETVAEIERQL QTLPTADVAK VAWEEHGMII 

       310        320        330        340        350        360 
LVDDLAEAVV EADKLAYEHV QVLTENPNYF LDHMTNYGAL FLGPETNVAY GDKVIGTNHT 

       370        380        390        400        410        420 
LPTKKAAKYT GGLWVGKFLK NCTYQRCTPE ASAEIGRIAE RLCELEGFIG HKAQASLRVK 


RYGK 

Q5WIU9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!