Entry Information
Protein Name GdhA
Accession No P00370
Protein description NADP-specific glutamate dehydrogenase
pI/Mw (Da)
Theoretical Experimental
5.98/48581.37 5.96/45327
5.81/46385 (DIGE 4.5-6.5)
5.94/44524 (DIGE 4.5-6.5)
Protein function and expression Decreases during phosphate limitation. May be directly degraded by ClpAP or ClpXP, respectively, or be modulated by a protease-dependent mechanism.
Reference(s) Lopez-Campistrous, A., P. Semchuk, L. Burke, T. Palmer-Stone, S. J. Brokx, G. Broderick, D. Bottorff, S. Bolch, J. H. Weiner, and M. J. Ellison. 2005. Localization, annotation & comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell. Proteomics 4:1205-1209. (NCBI)

Pasquali, C., S. Frutiger, M. R. Wilkins, G. J. Hughes, R. D. Appel, A. Bairoch, D. Schaller, J. C. Sanchez, and D. F. Hochstrasser. 1996. Two-dimensional gel electrophoresis of Escherichia coli homogenates: the Escherichia coli SWISS-2DPAGE database. Electrophoresis 17:547-555. (NCBI)

VanBogelen, R. A., E. R. Olson, B. L. Wanner, and F. C. Neidhardt. 1996. Global analysis of proteins synthesized during phosphorus restriction in Escherichia coli. J. Bacteriol. 178:4344-4366. (NCBI)

Vanbogelen, R. A., K. Z. Abshire, A. Pertsemlidis, R. L. Clark, and F. C. Neidhardt. 1996. Gene-protein database of Escherichia coli K-12, p 2067-2117. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology, 2nd ed., vol. 1. ASM Press, Washington, D.C. (NCBI)

Weichart, D., N. Querfurth, M. Dreger, and R. Hengge-Aronis. 2003. Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coli. J. Bacteriol. 185:115-125. (NCBI)

Yan, J. X., A. T. Devenish, R. Wait, T. Stone, S. Lewis, and S. Fowler. 2002. Fluorescence two-dimensional difference gel electrophoresis and mass spectrometry based proteomic analysis of Escherichia coli. Proteomics 2:1682-1698. (NCBI)

2D gels information
Map ID38
Reference(s)Champion, K. M., J. C. Nishihara, J. C. Joly, and D. Arnott. 2001. Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes. Proteomics 1:1133-1148. (NCBI)
Protein function and expression(s)Map: A
pI/Mw: 6.03/45028

A
2-DE profile of E. coli proteins at the end of anti-CD18 blank run fermentation.
Map ID325
Reference(s)Yoon, S. H., M. -J. Han, S. Y. Lee, K. J. Jeong, and J. -S. Yoo. 2003. Combined transcriptome and proteome analysis of Escherichia coli during high cell density culture. Biotechnol. Bioeng. 81:753-767. (NCBI)
Protein function and expression(s)Map: A B C D E F G


A
Two-dimensional protein expression map. Protens that identified by MALDI-TOF MS are labeled with red, and those identified by E. coli SWISS-2DPAGE are labeled with blue. E. coli W3110 0.88 g DCW/L.
B
Two-dimensional protein expression map. Protens that identified by MALDI-TOF MS are labeled with red, and those identified by E. coli SWISS-2DPAGE are labeled with blue. E. coli W3110 3.5 g DCW/L.
C
Two-dimensional protein expression map. Protens that identified by MALDI-TOF MS are labeled with red, and those identified by E. coli SWISS-2DPAGE are labeled with blue. E. coli W3110 12.7 g DCW/L.
D
Two-dimensional protein expression map. Protens that identified by MALDI-TOF MS are labeled with red, and those identified by E. coli SWISS-2DPAGE are labeled with blue. E. coli W3110 40 g DCW/L.
E
Two-dimensional protein expression map. Protens that identified by MALDI-TOF MS are labeled with red, and those identified by E. coli SWISS-2DPAGE are labeled with blue. E. coli W3110 62 g DCW/L.
F
Two-dimensional protein expression map. Protens that identified by MALDI-TOF MS are labeled with red, and those identified by E. coli SWISS-2DPAGE are labeled with blue. E. coli W3110 72 g DCW/L.
G
Two-dimensional protein expression map. Protens that identified by MALDI-TOF MS are labeled with red, and those identified by E. coli SWISS-2DPAGE are labeled with blue. E. coli W3110 74 g DCW/L.
Swiss-Prot Database Reference

Entry information
Entry Name DHE4_ECOLI
Primary accession number P00370
Secondary accession numbers P78173 
Integrated into Swiss-Prot on 1986-07-21
Sequence was last modified on 1986-07-21 (Sequence version 1)
Annotations were last modified on 2006-07-11 (Entry version 53)
Name and origin of the protein
Protein name NADP-specific glutamate dehydrogenase
Synonyms EC 1.4.1.4 NADP-specific glutamate dehydrogenase
NADP-GDH
Gene name Name : gdhA
OrderedLocusName : b1761
From Escherichia coli [TaxID:562] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia;
References
[1] NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-36.
strain = K12
PubMed=6308576[NCBI, ExPASy, EBI, Israel, Japan]
McPherson M.J. , Wootton J.C. ,
"Complete nucleotide sequence of the Escherichia coli gdhA gene."
Nucleic Acids Res.11:5257-5266(1983) 
[2] NUCLEOTIDE SEQUENCE [GENOMIC DNA].DOI=10.1016/0378-1119(84)90140-9;PubMed=6373501[NCBI, ExPASy, EBI, Israel, Japan]
Valle F. , Becerril B. , Chen E. , Seeburg P.H. , Heyneker H. , Bolivar F. ,
"Complete nucleotide sequence of the glutamate dehydrogenase gene from Escherichia coli K-12."
Gene27:193-199(1984) 
[3] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / W3110 / ATCC 27325 / DSM 5911
DOI=10.1093/dnares/3.6.363;PubMed=9097039[NCBI, ExPASy, EBI, Israel, Japan]
Aiba H. , Baba T. , Fujita K. , Hayashi K. , Inada T. , Isono K. , Itoh T. , Kasai H. , Kashimoto K. , Kimura S. , Kitakawa M. , Kitagawa M. , Makino K. , Miki T. , Mizobuchi K. , Mori H. , Mori T. , Motomura K. , Nakade S. , Nakamura Y. , Nashimoto H. , Nishio Y. , Oshima T. , Saito N. , Sampei G. , Seki Y. , Sivasundaram S. , Tagami H. , Takeda J. , Takemoto K. , Takeuchi Y. , Wada C. , Yamamoto Y. , Horiuchi T. ,
"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
DNA Res.3:363-377(1996) 
[4] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / MG1655 / ATCC 47076
DOI=10.1126/science.277.5331.1453;PubMed=9278503[NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R. , Plunkett G. III , Bloch C.A. , Perna N.T. , Burland V. , Riley M. , Collado-Vides J. , Glasner J.D. , Rode C.K. , Mayhew G.F. , Gregor J. , Davis N.W. , Kirkpatrick H.A. , Goeden M.A. , Rose D.J. , Mau B. , Shao Y. ,
"The complete genome sequence of Escherichia coli K-12."
Science277:1453-1474(1997) 
[5] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / W3110 / ATCC 27325 / DSM 5911
DOI=10.1038/msb4100049;
Hayashi K. , Morooka N. , Yamamoto Y. , Fujita K. , Isono K. , Choi S. , Ohtsubo E. , Baba T. , Wanner B.L. , Mori H. , Horiuchi T. ,
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Mol. Syst. Biol.2:E1-E5(2006) 
[6] PROTEIN SEQUENCE OF 1-12.
strain = K12 / EMG2
PubMed=9298646[NCBI, ExPASy, EBI, Israel, Japan]
Link A.J. , Robison K. , Church G.M. ,
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Electrophoresis18:1259-1313(1997) 
Comments
  • CATALYTIC ACTIVITY : L-glutamate + H(2)O + NADP(+) = 2-oxoglutarate + NH(3) + NADPH
  • SUBUNIT : Homohexamer
  • SIMILARITY : Belongs to the Glu/Leu/Phe/Val dehydrogenases family
  • Copyright
    Copyrighted by the UniProt Consortium, see http://www.uniprot.org/. Distributed under the Creative Commons Attribution-NoDerivs License.
    Cross-reference
    Sequence databases
    EMBL J01615;AAA87979.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    K02499;AAA23868.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    U00096;AAC74831.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    AP009048;BAA15550.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    PIR A00382;DEECEN.
    3D structure databases
    HSSP P24295;1AUP[HSSP ENTRY / PDB].
    ModBase P00370
    Protein-protein interaction databases
    DIP P00370
    Enzyme and pathway databases
    BioCyc EcoCyc:GDHA-MONOMER;-.
    2D gel databases
    SWISS-2DPAGE P00370;COLI.
    Organism-specific gene databases
    EchoBASE EB0367;-.
    ECO2DBASE G043.6;6TH EDITION.
    G043.7;6TH EDITION.
    EcoGene EG10372;gdhA.
    HOGENOM [Family / Alignment / Tree]
    Family and domain databases
    InterPro IPR006095;GLFV_DH.
    IPR006096;GLFV_DH_C.
    IPR006097;GLFV_DH_N.
    Graphical view of domain structure
    Pfam PF00208;ELFV_dehydrog;1.
    PF02812;ELFV_dehydrog_N;1.
    Pfam graphical view of domain structure
    PRINTS PR00082;GLFDHDRGNASE.
    BLOCKS P00370
    PROSITE PS00074;GLFV_DEHYDROGENASE;1.
    Genome annotation databases
    GenomeReviews U00096_GR;b1761.
    Other
    ProtoNet P00370
    UniRef View cluster of proteins with at least 50% / 90% / 100% identity
    Keyword
    Complete proteome; Direct protein sequencing; NADP; Oxidoreductase;
    Features
    Feature table viewer Feature aligner
    Key  From   To Length  Description  FTId
    CHAIN    1   447    447  NADP-specific glutamate dehydrogenase  PRO_0000182769
    ACT_SITE  128   128    (by similarity)  
    CONFLICT  385   385    A -> P: (in Ref. 2)  
    Sequence information
    Length: 447AA [This is the length of the unprocessed precursor] Molecular weight: 48581Da [This is the MW of the unprocessed precursor] CRC64: 7CB861D282C533C6[This is a checksum on the sequence]
            10         20         30         40         50         60
    MDQTYSLESF LNHVQKRDPN QTEFAQAVRE VMTTLWPFLE QNPKYRQMSL LERLVEPERV
            70         80         90        100        110        120
    IQFRVVWVDD RNQIQVNRAW RVQFSSAIGP YKGGMRFHPS VNLSILKFLG FEQTFKNALT
           130        140        150        160        170        180
    TLPMGGGKGG SDFDPKGKSE GEVMRFCQAL MTELYRHLGA DTDVPAGDIG VGGREVGFMA
           190        200        210        220        230        240
    GMMKKLSNNT ACVFTGKGLS FGGSLIRPEA TGYGLVYFTE AMLKRHGMGF EGMRVSVSGS
           250        260        270        280        290        300
    GNVAQYAIEK AMEFGARVIT ASDSSGTVVD ESGFTKEKLA RLIEIKASRD GRVADYAKEF
           310        320        330        340        350        360
    GLVYLEGQQP WSLPVDIALP CATQNELDVD AAHQLIANGV KAVAEGANMP TTIEATELFQ
           370        380        390        400        410        420
    QAGVLFAPGK AANAGGVATS GLEMAQNAAR LGWKAEKVDA RLHHIMLDIH HACVEHGGEG
           430        440 
    EQTNYVQGAN IAGFVKVADA MLAQGVI
    P00370 in FASTA format