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UniProtKB/Swiss-Prot entry Q8G2R2

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

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Entry information
Entry name HISX_BRUSU
Primary accession number Q8G2R2
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: BR0252
From
Brucella suis [TaxID: 29461] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Brucellaceae; Brucella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1330 / Biovar 1;
DOI=10.1073/pnas.192319099; PubMed=12271122 [NCBI, ExPASy, EBI, Israel, Japan]
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts.";
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(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
AE014291; AAN29201.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_697286.1; -.
3D structure databases
HSSP P06988; 1KAE. [HSSP ENTRY / PDB]
ModBase Q8G2R2.
Enzyme and pathway databases
BioCyc BSUI204722:BR_0252-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 1165911; -.
GenomeReviews AE014291_GR; BR0252.
KEGG bms:BR0252; -.
NMPDR fig|204722.1.peg.243; -.
TIGR BR0252; -.
Phylogenomic databases
HOGENOM Q8G2R2; -.
Other
ProtoNet Q8G2R2.
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_0000135741
ACT_SITE   327   327        Proton acceptor (By similarity). 
ACT_SITE   328   328        Proton acceptor (By similarity). 
METAL   259   259        Zinc (By similarity). 
METAL   262   262        Zinc (By similarity). 
METAL   361   361        Zinc (By similarity). 
METAL   420   420        Zinc (By similarity). 
BINDING   130   130        NAD (By similarity). 
BINDING   191   191        NAD (By similarity). 
BINDING   214   214        NAD (By similarity). 
BINDING   237   237        Substrate (By similarity). 
BINDING   259   259        Substrate (By similarity). 
BINDING   262   262        Substrate (By similarity). 
BINDING   328   328        Substrate (By similarity). 
BINDING   361   361        Substrate (By similarity). 
BINDING   415   415        Substrate (By similarity). 
BINDING   420   420        Substrate (By similarity). 
Sequence information
Length: 430 AA [This is the length of the unprocessed precursor] Molecular weight: 46072 Da [This is the MW of the unprocessed precursor] CRC64: 2752FA59731001E0 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MVTTLRQTDP DFEQKFAAFL SGKREVSEDV DRAVREIVDR VRREGDSALL DYSRRFDRID 

        70         80         90        100        110        120 
LEKTGIAVTE AEIDAAFDAA PASTVEALKL ARDRIEKHHA RQLPKDDRYT DALGVELGSR 

       130        140        150        160        170        180 
WTAIEAVGLY VPGGTASYPS SVLMNAMPAK VAGVDRIVMV VPAPDGNLNP LVLVAARLAG 

       190        200        210        220        230        240 
VSEIYRVGGA QAIAALAYGT ETIRPVAKIV GPGNAYVAAA KRIVFGTVGI DMIAGPSEVL 

       250        260        270        280        290        300 
IVADKDNNPD WIAADLLAQA EHDTAAQSIL MTNDEAFAHA VEEAVERQLH TLARTETASA 

       310        320        330        340        350        360 
SWRDFGAVIL VKDFEDAIPL ANRIAAEHLE IAVADAEAFV PRIRNAGSIF IGGYTPEVIG 

       370        380        390        400        410        420 
DYVGGCNHVL PTARSARFSS GLSVLDYMKR TSLLKLGSEQ LRALGPAAIE IARAEGLDAH 

       430 
AQSVAIRLNL
Q8G2R2 in FASTA format

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