CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002617
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Isocitrate dehydrogenase [NADP] 
Protein Synonyms/Alias
 IDH; IDP; NADP(+)-specific ICDH; Oxalosuccinate decarboxylase 
Gene Name
 icd 
Gene Synonyms/Alias
 icdA; icdE; b1136; JW1122 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
4****MESKVVVPAQGacetylation[1]
4****MESKVVVPAQGpupylation[2]
12VVVPAQGKKITLQNGacetylation[1]
13VVPAQGKKITLQNGKacetylation[1]
20KITLQNGKLNVPENPacetylation[1]
55VVDAAVEKAYKGERKacetylation[1, 3]
58AAVEKAYKGERKISWacetylation[3]
142QGTPSPVKHPELTDMacetylation[1, 3, 4, 5]
166IYAGIEWKADSADAEacetylation[1]
174ADSADAEKVIKFLREacetylation[1]
177ADAEKVIKFLREEMGacetylation[1, 5]
186LREEMGVKKIRFPEHacetylation[1]
199EHCGIGIKPCSEEGTacetylation[1]
230DSVTLVHKGNIMKFTacetylation[1, 5]
235VHKGNIMKFTEGAFKacetylation[1, 3, 5]
242KFTEGAFKDWGYQLAacetylation[1, 3, 5]
265IDGGPWLKVKNPNTGacetylation[1, 5]
267GGPWLKVKNPNTGKEacetylation[1]
273VKNPNTGKEIVIKDVacetylation[1]
273VKNPNTGKEIVIKDVpupylation[2]
350PKYAGQDKVNPGSIIacetylation[1, 3]
378EAADLIVKGMEGAINacetylation[1, 5]
387MEGAINAKTVTYDFEacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli.
 Cerda-Maira FA, McAllister F, Bode NJ, Burns KE, Gygi SP, Darwin KH.
 EMBO Rep. 2011 Jul 8;12(8):863-70. [PMID: 21738222]
 [3] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [4] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [5] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508
Functional Description
  
Sequence Annotation
 NP_BIND 339 345 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
 BINDING 391 391 NADP.
 BINDING 395 395 NADP.
 MOD_RES 100 100 N6-succinyllysine.
 MOD_RES 113 113 Phosphoserine.
 MOD_RES 142 142 N6-acetyllysine.
 MOD_RES 242 242 N6-succinyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP; Oxidoreductase; Phosphoprotein; Reference proteome; Tricarboxylic acid cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 416 AA 
Protein Sequence
MESKVVVPAQ GKKITLQNGK LNVPENPIIP YIEGDGIGVD VTPAMLKVVD AAVEKAYKGE 60
RKISWMEIYT GEKSTQVYGQ DVWLPAETLD LIREYRVAIK GPLTTPVGGG IRSLNVALRQ 120
ELDLYICLRP VRYYQGTPSP VKHPELTDMV IFRENSEDIY AGIEWKADSA DAEKVIKFLR 180
EEMGVKKIRF PEHCGIGIKP CSEEGTKRLV RAAIEYAIAN DRDSVTLVHK GNIMKFTEGA 240
FKDWGYQLAR EEFGGELIDG GPWLKVKNPN TGKEIVIKDV IADAFLQQIL LRPAEYDVIA 300
CMNLNGDYIS DALAAQVGGI GIAPGANIGD ECALFEATHG TAPKYAGQDK VNPGSIILSA 360
EMMLRHMGWT EAADLIVKGM EGAINAKTVT YDFERLMDGA KLLKCSEFGD AIIENM 416 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:EcoliWiki.
 GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0051287; F:NAD binding; IEA:InterPro.
 GO:0022900; P:electron transport chain; IMP:EcoliWiki.
 GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
 GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. 
Interpro
 IPR019818; IsoCit/isopropylmalate_DH_CS.
 IPR001804; Isocitrate/isopropylmalate_DH.
 IPR004439; Isocitrate_DH_NADP_dimer_prok.
 IPR024084; IsoPropMal-DH-like_dom. 
Pfam
 PF00180; Iso_dh 
SMART
  
PROSITE
 PS00470; IDH_IMDH 
PRINTS