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SWISS-2DPAGE 
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Sample Preparation and Post-separation Analysis



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




SWISS-2DPAGE:  GLTD_ECOLI


GLTD_ECOLI


General information about the entry
View entry in simple text format
Entry nameGLTD_ECOLI
Primary accession numberP09832
integrated into SWISS-2DPAGE on August 1, 1995 (release 2)
2D Annotations were last modified onOctober 1, 2001 (version 3)
General Annotations were last modified on May 19, 2011 (version 11)
Name and origin of the protein
DescriptionRecName: Full=Glutamate synthase [NADPH] small chain; EC=1.4.1.13; AltName: Full=Glutamate synthase subunit beta; Short=GLTS beta chain; AltName: Full=NADPH-GOGAT;.
Gene nameName=gltD
Synonyms=aspB
OrderedLocusNames=b3213, JW3180
Annotated speciesEscherichia coli [TaxID: 562]
TaxonomyBacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
References
[1]   MAPPING ON GEL
MEDLINE=96314059; PubMed=8740179; [NCBI, ExPASy, EBI, Israel, Japan]
Pasquali C., Frutiger S., Wilkins M.R., Hughes G.J., Appel R.D., Bairoch A., Schaller D., Sanchez J.-C., Hochstrasser D.F.
''''''Two-dimensional gel electrophoresis of Escherichia coli homogenates: the Escherichia coli SWISS-2DPAGE database'';'';''
Electrophoresis 17(1):547-555(1996)
[2]   MAPPING ON GEL
MEDLINE=83270974; PubMed=6308410; [NCBI, ExPASy, EBI, Israel, Japan]
Neidhardt F.C., Vaughn V., Phillips T.A., Bloch P.L.
''''''Gene-protein index of Escherichia coli K-12'';'';''
Microbiol. Rev. 47(1):231-284(1983)
[3]   MAPPING ON GEL
Vanbogelen R.A., Abshire K.Z., Pertsemlidis A., Clark R.L., Neidhardt F.C.
''''''Gene-protein database of Escherichia coli K-12, edition 6'';'';''
(IN) Neidhardt et al. (eds.)Escherichia coli and Salmonella: Cellular and Molecular Biology (2nd ed.), pp.2067-2117, ASM Press, Washington DC (1996)
[4]   MAPPING ON GEL
MEDLINE=98410772; PubMed=9740056; [NCBI, ExPASy, EBI, Israel, Japan]
Tonella L., Walsh B.J., Sanchez J.-C., Ou K., Wilkins M.R., Tyler M., Frutiger S., Gooley A.A., Pescaru I., Appel R.D., Yan J.X., Bairoch A., Hoogland C., Morch F.S., Hughes G.J., Williams K.L., Hochstrasser D.F.
'''''''98 Escherichia coli SWISS-2DPAGE database update'';'';''
Electrophoresis 19(1):1960-1971(1998)
[5]   PROTEIN EXPRESSION
MEDLINE=92138602; PubMed=1346534; [NCBI, ExPASy, EBI, Israel, Japan]
Ernsting B.R., Atkinson M.R., Ninfa A.J., Matthews R.G.
''''''Characterization of the regulon controlled by the leucine-responsive regulatory protein in Escherichia coli'';'';''
J. Bacteriol. 174(1):1109-1118(1992)
[6]   MAPPING ON GEL
PubMed=11680886; [NCBI, ExPASy, EBI, Israel, Japan]
Tonella L., Hoogland C., Binz P.-A., Appel R.D., Hochstrasser D.F., Sanchez J.-C.
''''''New perspectives in the Escherichia coli proteome investigation'';'';''
Proteomics 1(1):409-423(2001)
Comments
  • SUBUNIT: AGGREGATE OF 4 CATALYTICAL ACTIVE HETERODIMERS
2D PAGE maps for identified proteins
How to interpret a protein

ECOLI {Escherichia coli}
Escherichia coli
ECOLI
  map experimental info
  protein estimated location
 
ECOLI

MAP LOCATIONS:
pI=5.40; Mw=52658  [identification data]
pI=5.47; Mw=52555

EXPRESSION:
AN APPROXIMATELY TWO-FOLD-LOWER GLUTAMATE SYNTHASE ACTIVITY WAS DETECTED WHEN LRP+ STRAINS WERE GROWN IN THE PRESENCE OF EXOGENOUS LEUCINE [5].

MAPPING (identification):
SPOT 2D-000KQL: AMINO ACID COMPOSITION AND SEQUENCE TAG (SQNV) [4];
SPOT 2D-000KQS: GEL MATCHING [1] AND IDENTIFIED ON 2-D GELS BY NEIDHARDT [2] AND VANBOGELEN [3].



ECOLI5-6 {Escherichia coli(5-6)}
Escherichia coli
ECOLI5-6
  map experimental info
  protein estimated location
 
ECOLI5-6

MAP LOCATIONS:
pI=5.48; Mw=53050  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [6].

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 legal@sib.swiss).
Cross-references
ECO2DBASEF050.4; 6TH EDITION.
UniProtKB/Swiss-ProtP09832; GLTD_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 nameGLTD_ECOLI
Primary accession numberP09832
Secondary accession number(s) Q2M8Z9
Sequence was last modified on January 23, 2007 (version 3)
Annotations were last modified on October 19, 2011 (version 123)
Name and origin of the protein
DescriptionRecName: Full=Glutamate synthase [NADPH] small chain; EC=1.4.1.13; AltName: Full=Glutamate synthase subunit beta; Short=GLTS beta chain; AltName: Full=NADPH-GOGAT;
Gene nameName=gltD
Synonyms=aspB
OrderedLocusNames=b3213, JW3180
Encoded onName=gltD; Synonyms=aspB; OrderedLocusNames=b3213, JW3180
Keywords4Fe-4S; Amino-acid biosynthesis; Complete proteome; Direct protein sequencing; Glutamate biosynthesis; Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase; Reference proteome.
Copyright
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLM18747; AAA23905.1; -; Genomic_DNA
EMBLU18997; AAA58015.1; -; Genomic_DNA
EMBLU00096; AAC76245.1; -; Genomic_DNA
EMBLAP009048; BAE77257.1; -; Genomic_DNA
PIRG65112; G65112; .
RefSeqNP_417680.1; NC_000913.2; .
ProteinModelPortalP09832; -; .
SMRP09832; 3-471; .
DIPDIP-9803N; -; .
IntActP09832; 6; .
MINTMINT-1248739; -; .
SWISS-2DPAGEP09832; -; .
ECO2DBASEF050.4; 6TH EDITION; .
EnsemblBacteriaEBESCT00000004091; EBESCP00000004091; EBESCG00000003342; .
EnsemblBacteriaEBESCT00000017797; EBESCP00000017088; EBESCG00000016853; .
GeneID947723; -; .
GenomeReviewsAP009048_GR; JW3180; .
GenomeReviewsU00096_GR; b3213; .
KEGGecj:JW3180; -; .
KEGGeco:b3213; -; .
EchoBASEEB0399; -; .
EcoGeneEG10404; gltD; .
eggNOGCOG0493; -; .
GeneTreeEBGT00050000009108; -; .
HOGENOMHBG715033; -; .
OMAENMPGSK; -; .
ProtClustDBPRK12810; -; .
BioCycEcoCyc:GLUSYNSMALL-MONOMER; -; .
BioCycMetaCyc:GLUSYNSMALL-MONOMER; -; .
BRENDA1.4.1.13; 2026; .
GenevestigatorP09832; -; .
GOGO:0051539; F:4 iron; 4 sulfur cluster binding; IEA:UniProtKB-KW
GOGO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro; .
GOGO:0004355; F:glutamate synthase (NADPH) activity; IDA:EcoCyc; .
GOGO:0046872; F:metal ion binding; IEA:UniProtKB-KW; .
GOGO:0005515; F:protein binding; IPI:IntAct; .
GOGO:0006537; P:glutamate biosynthetic process; IDA:EcoCyc; .
InterProIPR017896; 4Fe4S_Fe-S-bd; .
InterProIPR012285; Fum_reductase_C; .
InterProIPR006006; Glut_synth_ssu2; .
InterProIPR009051; Helical_ferredxn; .
InterProIPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD; .
InterProIPR001327; Pyr_OxRdtase_NAD-bd_dom; .
Gene3DG3DSA:1.10.1060.10; Fum_reductase_C; 1; .
PfamPF00070; Pyr_redox; 1; .
PfamPF07992; Pyr_redox_2; 1; .
SUPFAMSSF46548; Helical_ferredxn; 1; .
TIGRFAMsTIGR01318; GltD_gamma_fam; 1; .
PROSITEPS51379; 4FE4S_FER_2; 1; .



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Database constructed and maintained by SIB, using the Make2D-DB II package (ver. 3.10.2) from the World-2DPAGE Constellation of the ExPASy web server