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UniProtKB/Swiss-Prot entry P59398

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

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Entry information
Entry name HISX_BUCBP
Primary accession number P59398
Secondary accession numbers None
Integrated into Swiss-Prot on March 25, 2003
Sequence was last modified on March 25, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 44)
Name and origin of the protein
Protein name Histidinol dehydrogenase
Synonyms HDH
EC 1.1.1.23
Gene name
Name: hisD
OrderedLocusNames: bbp_094
From
Buchnera aphidicola subsp. Baizongia pistaciae [TaxID: 135842] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0235981100; PubMed=12522265 [NCBI, ExPASy, EBI, Israel, Japan]
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
"Reductive genome evolution in Buchnera aphidicola.";
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(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
AE016826; AAO26829.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_777724.1; -.
3D structure databases
HSSP P06988; 1KAE. [HSSP ENTRY / PDB]
ModBase P59398.
Enzyme and pathway databases
BioCyc BAPH224915:BBP_094-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 P59398.
Genome annotation databases
GeneID 1058171; -.
GenomeReviews AE016826_GR; bbp_094.
KEGG bab:bbp094; -.
Phylogenomic databases
HOGENOM P59398; -.
Genome annotation databases
CMR P59398; bbp_094.
Other
ProtoNet P59398.
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   435  435     Histidinol dehydrogenase. PRO_0000135743
ACT_SITE   327   327        Proton acceptor (By similarity). 
ACT_SITE   328   328        Proton acceptor (By similarity). 
METAL   260   260        Zinc (By similarity). 
METAL   263   263        Zinc (By similarity). 
METAL   361   361        Zinc (By similarity). 
METAL   420   420        Zinc (By similarity). 
BINDING   131   131        NAD (By similarity). 
BINDING   189   189        NAD (By similarity). 
BINDING   212   212        NAD (By similarity). 
BINDING   238   238        Substrate (By similarity). 
BINDING   260   260        Substrate (By similarity). 
BINDING   263   263        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: 435 AA [This is the length of the unprocessed precursor] Molecular weight: 48185 Da [This is the MW of the unprocessed precursor] CRC64: 8A2F3ED2073D73F2 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MEVYIPIIYW KSCSEKEKRE ILFRPVVNDN SQIKEVVKEI ITNVKNSGDK ALYDYTKTFD 

        70         80         90        100        110        120 
KIRLESIQVS YGEIVDSDSF VNEEIQKSIS VAKNNIKIFH EKQTHNVVNI EIQPGVFCRQ 

       130        140        150        160        170        180 
IIRPIQSVGL YIPGGCAPLV STVLMLAIPA KIVGCKNIIL CSPPPITKEI LYASKICGIH 

       190        200        210        220        230        240 
NIFQVGGAQA IAAMAFGTKT IPKVNKIFGP GNVYVTEAKL QINALLNDLS IDMLAGPSEI 

       250        260        270        280        290        300 
LIIADFKANA CIIASDFLSQ MEHGIYSQAI LVTPSYDLAC NVIFEINIQL KNLSRKKVIN 

       310        320        330        340        350        360 
KSLKYSRIIV TKTLLECFEI SNLYAPEHLI IQCENSNRLL VYVINAGSIF LGRWSAVASG 

       370        380        390        400        410        420 
DYVTGTNHVL PTYGSAIVNS GLTVMDFQKI ISVQKLDQQG LIDVSSSIIS LSEVERMDAH 

       430 
TNSIKQRLIA LQDVK
P59398 in FASTA format

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