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UniProtKB/Swiss-Prot entry Q8G4S9

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

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Entry information
Entry name HISX_BIFLO
Primary accession number Q8G4S9
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    July 22, 2008 (Entry version 39)
Name and origin of the protein
Protein name Histidinol dehydrogenase
Synonyms HDH
EC 1.1.1.23
Gene name
Name: hisD
OrderedLocusNames: BL1295
From
Bifidobacterium longum [TaxID: 216816] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; Bifidobacteriaceae; Bifidobacterium.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCC 2705;
DOI=10.1073/pnas.212527599; PubMed=12381787 [NCBI, ExPASy, EBI, Israel, Japan]
Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract.";
Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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
AE014295; AAN25096.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_696460.1; -.
3D structure databases
HSSP P06988; 1KAE. [HSSP ENTRY / PDB]
ModBase Q8G4S9.
Enzyme and pathway databases
BioCyc BLON206672:BL1295-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 Q8G4S9.
Genome annotation databases
GeneID 1022774; -.
GenomeReviews AE014295_GR; BL1295.
KEGG blo:BL1295; -.
NMPDR fig|206672.1.peg.1227; -.
Phylogenomic databases
HOGENOM Q8G4S9; -.
Genome annotation databases
CMR Q8G4S9; BL1295.
Other
ProtoNet Q8G4S9.
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   471  471     Histidinol dehydrogenase. PRO_0000135733
ACT_SITE   350   350        Proton acceptor (By similarity). 
ACT_SITE   351   351        Proton acceptor (By similarity). 
METAL   281   281        Zinc (By similarity). 
METAL   284   284        Zinc (By similarity). 
METAL   384   384        Zinc (By similarity). 
METAL   443   443        Zinc (By similarity). 
BINDING   139   139        NAD (By similarity). 
BINDING   204   204        NAD (By similarity). 
BINDING   236   236        NAD (By similarity). 
BINDING   259   259        Substrate (By similarity). 
BINDING   281   281        Substrate (By similarity). 
BINDING   284   284        Substrate (By similarity). 
BINDING   351   351        Substrate (By similarity). 
BINDING   384   384        Substrate (By similarity). 
BINDING   438   438        Substrate (By similarity). 
BINDING   443   443        Substrate (By similarity). 
Sequence information
Length: 471 AA [This is the length of the unprocessed precursor] Molecular weight: 50257 Da [This is the MW of the unprocessed precursor] CRC64: 36D6D724978BDC88 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLRWGVMSEN IMRIIDLRGQ NLSRAELLAA MPRAAMGTSE ATDLVRPILD DVKERGAAAL 

        70         80         90        100        110        120 
RDFEEKFDHV RPKNLRVPVE AIKDALTTLD PEVRAAIEES VRRARAVAAN QVPKDFYTDL 

       130        140        150        160        170        180 
AEGARVAERW IPIQRVGLYV PGGKAVYPSS VIMNAVPAQA AGVESLAIAT PPARDNEEGL 

       190        200        210        220        230        240 
PNKTILATCA ILGVDEVYAV GGAQAIAMFA YGAKGSEPQD GDILCDPVDK ITGPGNIFVA 

       250        260        270        280        290        300 
TAKSLVSAFV GIDAVAGPTE IGIIADETAN PSLLAADLIG QAEHDELAGS VLFTDSTEIA 

       310        320        330        340        350        360 
DKVQESLKYR VPRTEHAERV HTSLSGTQSA IVLTDGLDQS IDAANAYAAE HLEIQTKDAD 

       370        380        390        400        410        420 
AVVKRIKNAG AIFRGPYSPV PLGDYMSGSN HVLPTGGTAR FAAGLGVHTF MKPVEVIEYD 

       430        440        450        460        470 
EEGLKALAAR INAFAVSEDL PAHGECVLSR FVKDPYDKAT LREQEKEAGL R
Q8G4S9 in FASTA format

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