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Sample Preparation and Post-separation Analysis



Searching in 'SWISS-2DPAGE' for entry matching: P06988




SWISS-2DPAGE:  P06988


P06988


General information about the entry
View entry in simple text format
Entry nameHISX_ECOLI
Primary accession numberP06988
integrated into SWISS-2DPAGE on May 15, 2003 (release 16)
2D Annotations were last modified onMay 15, 2003 (version 1)
General Annotations were last modified on May 19, 2011 (version 6)
Name and origin of the protein
DescriptionRecName: Full=Histidinol dehydrogenase; Short=HDH; EC=1.1.1.23;.
Gene nameName=hisD
OrderedLocusNames=b2020, JW2002
Annotated speciesEscherichia coli [TaxID: 562]
TaxonomyBacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
References
[1]   MAPPING ON GEL
PubMed=12469338; [NCBI, ExPASy, EBI, Israel, Japan]
Yan J.X., Devenish A.T., Wait R., Stone T., Lewis S., Fowler S.
''''''Fluorescence 2-D difference gel electrophoresis and mass spectrometry based proteomic analysis of E. coli'';'';''
Proteomics 2(1):1682-1698(2002)
Comments
  • SUBUNIT: HOMODIMER
2D PAGE maps for identified proteins
How to interpret a protein

ECOLI-DIGE4.5-6.5 {Escherichia coli DIGE (4.5-6.5)}
Escherichia coli
ECOLI-DIGE4.5-6.5
  map experimental info
  protein estimated location
 
ECOLI-DIGE4.5-6.5

MAP LOCATIONS:
pI=5.07; Mw=48837  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [1].

Copyright
This SWISS-2DPAGE entry is copyright the Swiss Institute of Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified and this statement is not removed. Usage by and for commercial entities requires a license agreement (See http://world-2dpage.expasy.org/swiss-2dpage/docs/license.html or send email from license@isb-sib.ch).
Cross-references
2DBase-EcoliP06988; HISX_ECOLI.
UniProtKB/Swiss-ProtP06988; HISX_ECOLI.
2D PAGE maps for identified proteins
  • How to interpret a protein map
  • You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw.
  • Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly.
  • Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed.



External data extracted from UniProtKB/Swiss-Prot
Extracted from UniProtKB/Swiss-Prot, release: 2011_10
Entry nameHISX_ECOLI
Primary accession numberP06988
Secondary accession number(s) O08506 P78076 Q47254
Sequence was last modified on January 23, 2007 (version 5)
Annotations were last modified on October 19, 2011 (version 120)
Name and origin of the protein
DescriptionRecName: Full=Histidinol dehydrogenase; Short=HDH; EC=1.1.1.23;
Gene nameName=hisD
OrderedLocusNames=b2020, JW2002
Encoded onName=hisD; OrderedLocusNames=b2020, JW2002
Keywords3D-structure; Amino-acid biosynthesis; Complete proteome; Direct protein sequencing; Histidine biosynthesis; Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLX13462; CAA31812.1; -; Genomic_DNA
EMBLX03972; CAA27610.1; -; Genomic_DNA
EMBLX52656; CAA36882.1; -; Genomic_DNA
EMBLU00096; AAC75081.1; -; Genomic_DNA
EMBLAP009048; BAA15851.1; -; Genomic_DNA
EMBLM10483; AAA23962.1; -; Genomic_DNA
PIRC64967; DEECHT; .
RefSeqNP_416524.1; NC_000913.2; .
PDB1K75; X-ray; 1.75 A; A/B=1-434
PDB1KAE; X-ray; 1.70 A; A/B=1-434
PDB1KAH; X-ray; 2.10 A; A/B=1-434
PDB1KAR; X-ray; 2.10 A; A/B=1-434
PDBsum1K75; -; .
PDBsum1KAE; -; .
PDBsum1KAH; -; .
PDBsum1KAR; -; .
ProteinModelPortalP06988; -; .
SMRP06988; 1-434; .
IntActP06988; 6; .
SWISS-2DPAGEP06988; -; .
2DBase-EcoliP06988; -; .
PRIDEP06988; -; .
EnsemblBacteriaEBESCT00000004611; EBESCP00000004611; EBESCG00000003760; .
EnsemblBacteriaEBESCT00000018150; EBESCP00000017441; EBESCG00000017205; .
GeneID946531; -; .
GenomeReviewsAP009048_GR; JW2002; .
GenomeReviewsU00096_GR; b2020; .
KEGGecj:JW2002; -; .
KEGGeco:b2020; -; .
EchoBASEEB0442; -; .
EcoGeneEG10447; hisD; .
eggNOGCOG0141; -; .
GeneTreeEBGT00050000009660; -; .
HOGENOMHBG329596; -; .
OMANRYVTEA; -; .
ProtClustDBPRK00877; -; .
BioCycEcoCyc:HISTDEHYD-MONOMER; -; .
BioCycMetaCyc:HISTDEHYD-MONOMER; -; .
GenevestigatorP06988; -; .
GOGO:0004399; F:histidinol dehydrogenase activity; IDA:EcoCyc; .
GOGO:0051287; F:NAD binding; IEA:InterPro; .
GOGO:0008270; F:zinc ion binding; IEA:InterPro; .
GOGO:0000105; P:histidine biosynthetic process; IDA:EcoCyc; .
HAMAPMF_01024; HisD; 1; -
InterProIPR016161; Ald_DH/histidinol_DH; .
InterProIPR001692; Histidinol_DH_CS; .
InterProIPR022695; Histidinol_DH_monofunct; .
InterProIPR012131; Hstdl_DH; .
PANTHERPTHR21256:SF2; Hstdl_DH_prok; 1; .
PfamPF00815; Histidinol_dh; 1; .
PIRSFPIRSF000099; Histidinol_dh; 1; .
PRINTSPR00083; HOLDHDRGNASE; .
SUPFAMSSF53720; Aldehyde_DH/Histidinol_DH; 1; .
TIGRFAMsTIGR00069; HisD; 1; .
PROSITEPS00611; HISOL_DEHYDROGENASE; 1; .



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