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UniProtKB/Swiss-Prot entry P08200


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

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Entry information
Entry name IDH_ECOLI
Primary accession number P08200
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on August 1, 1988 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 91)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NADP]
Synonyms IDH
EC 1.1.1.42
Oxalosuccinate decarboxylase
NADP(+)-specific ICDH
IDP
Gene name
Name: icd
Synonyms: icdA, icdE
OrderedLocusNames: b1136, JW1122
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3112144 [NCBI, ExPASy, EBI, Israel, Japan]
Thorsness P.E., Koshland D.E. Jr.;
"Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate.";
J. Biol. Chem. 262:10422-10425(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan]
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
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.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-414.
STRAIN=CH734;
PubMed=9352899 [NCBI, ExPASy, EBI, Israel, Japan]
Wang F.-S., Whittam T.S., Selander R.K.;
"Evolutionary genetics of the isocitrate dehydrogenase gene (icd) in Escherichia coli and Salmonella enterica.";
J. Bacteriol. 179:6551-6559(1997).
[6]
PROTEIN SEQUENCE OF 1-12.
STRAIN=K12 / EMG2;
DOI=10.1002/elps.1150180807; 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.";
Electrophoresis 18:1259-1313(1997).
[7]
ENZYME KINETICS, AND MUTAGENESIS OF TYR-160 AND LYS-230.
DOI=10.1021/bi00001a046; PubMed=7819221 [NCBI, ExPASy, EBI, Israel, Japan]
Lee M.E., Dyer D.H., Klein O.D., Bolduc J.M., Stoddard B.L., Koshland D.E. Jr.;
"Mutational analysis of the catalytic residues lysine 230 and tyrosine 160 in the NADP(+)-dependent isocitrate dehydrogenase from Escherichia coli.";
Biochemistry 34:378-384(1995).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M800187-MCP200; PubMed=18723842 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved modification in E. coli.";
Mol. Cell. Proteomics 0:0-0(2008).
[9]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ISOCITRATE AND MAGNESIUM, PHOSPHORYLATION AT SER-113, AND MUTAGENESIS OF SER-113.
PubMed=2204109 [NCBI, ExPASy, EBI, Israel, Japan]
Hurley J.H., Dean A.M., Sohl J.L., Koshland D.E. Jr., Stroud R.M.;
"Regulation of an enzyme by phosphorylation at the active site.";
Science 249:1012-1016(1990).
[10]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ISOCITRATE; NADP AND MAGNESIUM, MUTAGENESIS OF TYR-160 AND LYS-230, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=7761851 [NCBI, ExPASy, EBI, Israel, Japan]
Bolduc J.M., Dyer D.H., Scott W.G., Singer P., Sweet R.M., Koshland D.E. Jr., Stoddard B.L.;
"Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase.";
Science 268:1312-1318(1995).
[11]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NADP, AND SUBUNIT.
PubMed=2682654 [NCBI, ExPASy, EBI, Israel, Japan]
Hurley J.H., Thorsness P.E., Ramalingam V., Helmers N.H., Koshland D.E. Jr., Stroud R.M.;
"Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.";
Proc. Natl. Acad. Sci. U.S.A. 86:8635-8639(1989).
[12]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT MET-230.
DOI=10.1006/jmbi.1999.3195; PubMed=10623532 [NCBI, ExPASy, EBI, Israel, Japan]
Cherbavaz D.B., Lee M.E., Stroud R.M., Koshland D.E. Jr.;
"Active site water molecules revealed in the 2.1 A resolution structure of a site-directed mutant of isocitrate dehydrogenase.";
J. Mol. Biol. 295:377-385(2000).
[13]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT GLU-113 IN COMPLEX WITH SUBSTRATE ANALOG; MAGNESIUM AND NADP.
DOI=10.1021/bi002533q; PubMed=11284679 [NCBI, ExPASy, EBI, Israel, Japan]
Doyle S.A., Beernink P.T., Koshland D.E. Jr.;
"Structural basis for a change in substrate specificity: crystal structure of S113E isocitrate dehydrogenase in a complex with isopropylmalate, Mg2+, and NADP.";
Biochemistry 40:4234-4241(2001).
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
J02799; AAA24006.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74220.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA35958.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF017587; AAC45887.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A28482; DCECIS.
RefSeq AP_001762.1; -.
NP_415654.1; -.
3D structure databases
PDB
1AI2; X-ray; 1.90 A; A=1-416.[ExPASy / RCSB / EBI]
1AI3; X-ray; 1.90 A; A=1-416.[ExPASy / RCSB / EBI]
1BL5; X-ray; 2.50 A; A=3-416.[ExPASy / RCSB / EBI]
1CW1; X-ray; 2.10 A; A=1-416.[ExPASy / RCSB / EBI]
1CW4; X-ray; 2.10 A; A=1-416.[ExPASy / RCSB / EBI]
1CW7; X-ray; 2.60 A; A=1-416.[ExPASy / RCSB / EBI]
1GRO; X-ray; 2.50 A; A=1-416.[ExPASy / RCSB / EBI]
1GRP; X-ray; 2.50 A; A=1-416.[ExPASy / RCSB / EBI]
1HJ6; X-ray; 2.00 A; A=1-416.[ExPASy / RCSB / EBI]
1IDC; X-ray; 2.50 A; A=1-416.[ExPASy / RCSB / EBI]
1IDD; X-ray; 2.50 A; A=1-416.[ExPASy / RCSB / EBI]
1IDE; X-ray; 2.50 A; A=1-416.[ExPASy / RCSB / EBI]
1IDF; X-ray; 2.50 A; A=1-416.[ExPASy / RCSB / EBI]
1IKA; X-ray; 2.70 A; A=1-416.[ExPASy / RCSB / EBI]
1ISO; X-ray; 1.90 A; A=1-416.[ExPASy / RCSB / EBI]
1P8F; X-ray; 1.85 A; A=1-416.[ExPASy / RCSB / EBI]
1PB1; X-ray; 1.70 A; A=1-416.[ExPASy / RCSB / EBI]
1PB3; X-ray; 1.70 A; A=1-416.[ExPASy / RCSB / EBI]
1SJS; X-ray; 2.42 A; A=1-416.[ExPASy / RCSB / EBI]
3ICD; X-ray; 2.50 A; A=1-416.[ExPASy / RCSB / EBI]
4ICD; X-ray; 2.50 A; A=1-416.[ExPASy / RCSB / EBI]
5ICD; X-ray; 2.50 A; A=1-416.[ExPASy / RCSB / EBI]
6ICD; X-ray; 2.80 A; A=1-416.[ExPASy / RCSB / EBI]
7ICD; X-ray; 2.40 A; A=1-416.[ExPASy / RCSB / EBI]
8ICD; X-ray; 2.50 A; A=1-416.[ExPASy / RCSB / EBI]
9ICD; X-ray; 2.50 A; A=1-416.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AI2; -.
1AI3; -.
1BL5; -.
1CW1; -.
1CW4; -.
1CW7; -.
1GRO; -.
1GRP; -.
1HJ6; -.
1IDC; -.
1IDD; -.
1IDE; -.
1IDF; -.
1IKA; -.
1ISO; -.
1P8F; -.
1PB1; -.
1PB3; -.
1SJS; -.
3ICD; -.
4ICD; -.
5ICD; -.
6ICD; -.
7ICD; -.
8ICD; -.
9ICD; -.
ModBase P08200.
PTM databases
PhosSite P08200; -.
Enzyme and pathway databases
BioCyc EcoCyc:ISOCITDEH-SUBUNIT; -.
MetaCyc:ISOCITDEH-SUBUNIT; -.
2D gel databases
SWISS-2DPAGE P08200; -.
2DBase-Ecoli P08200; -.
ECO2DBASE C043.8; 6TH EDITION.
Organism-specific databases
EchoBASE EB0484; -.
EcoGene EG10489; icd.
EG10009; icdC.
Ontologies
GO
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006097; Biological process: glyoxylate cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR004439; IsoCit_DHase_NADP_prok.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11835; IDH_IMDH_dimeric; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00183; prok_nadp_idh; 1.
PROSITE PS00470; IDH_IMDH; 1.
BLOCKS P08200.
ProtoNet P08200.
Other
SWISS-3DIMAGE P08200.
Genome annotation databases
GeneID 945702; -.
GenomeReviews U00096_GR; b1136.
AP009048_GR; JW1122.
KEGG ecj:JW1122; -.
eco:b1136; -.
Phylogenomic databases
HOGENOM P08200; -.
Other
LinkHub P08200; -.
Genome annotation databases
CMR P08200; b1136.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP; Oxidoreductase; Phosphoprotein; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   416  416     Isocitrate dehydrogenase [NADP]. PRO_0000083551
NP_BIND   339   345  7     NADP. 
METAL   307   307        Magnesium or manganese. 
BINDING   104   104        NADP. 
BINDING   113   113        Substrate. 
BINDING   115   115        Substrate. 
BINDING   119   119        Substrate. 
BINDING   129   129        Substrate. 
BINDING   153   153        Substrate. 
BINDING   352   352        NADP; via amide nitrogen and carbonyl oxygen. 
BINDING   391   391        NADP. 
BINDING   395   395        NADP. 
SITE   160   160  1     Critical for catalysis. 
SITE   230   230  1     Critical for catalysis. 
MOD_RES   113   113        Phosphoserine. 
MOD_RES   142   142        N6-acetyllysine. 
MUTAGEN   113   113        S->D,E: Reduced affinity for isocitrate. 
MUTAGEN   160   160        Y->F: Large decrease in activity and a small increase in substrate affinity. 
MUTAGEN   230   230        K->M: Decrease in activity and substrate affinity. 
STRAND   15    17  3      
STRAND   20    22  3      
STRAND   25    32  8      
HELIX   38    57  20      
STRAND   64    67  4      
HELIX   72    78  7      
HELIX   86    95  10      
STRAND   96   100  5      
STRAND   107   109  3      
HELIX   114   121  8      
STRAND   126   132  7      
STRAND   140   142  3      
HELIX   144   146  3      
STRAND   148   154  7      
HELIX   159   161  3      
HELIX   170   181  12      
STRAND   194   202  9      
HELIX   203   219  17      
STRAND   223   229  7      
TURN   231   233  3      
TURN   235   237  3      
HELIX   238   253  16      
STRAND   264   267  4      
TURN   269   271  3      
STRAND   274   281  8      
HELIX   282   291  10      
HELIX   293   295  3      
STRAND   298   301  4      
HELIX   303   316  14      
TURN   320   322  3      
STRAND   326   328  3      
STRAND   333   336  4      
TURN   343   347  5      
HELIX   354   366  13      
HELIX   370   385  16      
HELIX   391   394  4      
HELIX   405   414  10      
Sequence information
Length: 416 AA [This is the length of the unprocessed precursor] Molecular weight: 45757 Da [This is the MW of the unprocessed precursor] CRC64: 9A02E707C3B4FDD9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MESKVVVPAQ GKKITLQNGK LNVPENPIIP YIEGDGIGVD VTPAMLKVVD AAVEKAYKGE 

        70         80         90        100        110        120 
RKISWMEIYT GEKSTQVYGQ DVWLPAETLD LIREYRVAIK GPLTTPVGGG IRSLNVALRQ 

       130        140        150        160        170        180 
ELDLYICLRP VRYYQGTPSP VKHPELTDMV IFRENSEDIY AGIEWKADSA DAEKVIKFLR 

       190        200        210        220        230        240 
EEMGVKKIRF PEHCGIGIKP CSEEGTKRLV RAAIEYAIAN DRDSVTLVHK GNIMKFTEGA 

       250        260        270        280        290        300 
FKDWGYQLAR EEFGGELIDG GPWLKVKNPN TGKEIVIKDV IADAFLQQIL LRPAEYDVIA 

       310        320        330        340        350        360 
CMNLNGDYIS DALAAQVGGI GIAPGANIGD ECALFEATHG TAPKYAGQDK VNPGSIILSA 

       370        380        390        400        410 
EMMLRHMGWT EAADLIVKGM EGAINAKTVT YDFERLMDGA KLLKCSEFGD AIIENM 

P08200 in FASTA format

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