CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006664
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aconitate hydratase 2 
Protein Synonyms/Alias
 Aconitase; 2-methylisocitrate dehydratase; Citrate hydro-lyase 
Gene Name
 acnB 
Gene Synonyms/Alias
 yacI; yacJ; b0118; JW0114 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
20AAEGIAPKPLDANQMacetylation[1]
77AIAKGEAKSPLLTPEacetylation[1]
77AIAKGEAKSPLLTPEpupylation[2]
85SPLLTPEKAIELLGTacetylation[3]
110IDALDDAKLAPIAAKacetylation[1]
117KLAPIAAKALSHTLLacetylation[3]
135NFYDVEEKAKAGNEYacetylation[1]
144KAGNEYAKQVMQSWAacetylation[1]
221PGVVGPIKQIEALQQacetylation[1]
229QIEALQQKGFPLAYVacetylation[1]
267DIPHVPNKRGGGLCLacetylation[1]
373SDVFRQAKDVAESDRacetylation[1]
387RGFSLAQKMVGRACGacetylation[1]
396VGRACGVKGIRPGAYacetylation[1, 3]
407PGAYCEPKMTSVGSQacetylation[1, 3]
537ESVLVRFKGKMQPGIacetylation[1]
539VLVRFKGKMQPGITLacetylation[1, 3]
559AIPLYAIKQGLLTVEacetylation[1, 3, 4]
567QGLLTVEKKGKKNIFacetylation[1]
571TVEKKGKKNIFSGRIacetylation[3]
588IEGLPDLKVEQAFELacetylation[1]
613GCTIKLNKEPIIEYLacetylation[1, 3]
728GKLLDAHKGQLPTRLacetylation[1, 3]
759GYYSVFGKSGARIEIacetylation[1]
835TYVAQVDKTAVDTYRacetylation[1, 3]
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] 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
 Catalyzes the isomerization of citrate to isocitrate via cis-aconitate as well as the dehydration of 2-methylisocitrate to cis-2-methylaconitate. 
Sequence Annotation
 REGION 244 246 Substrate binding.
 REGION 414 416 Substrate binding.
 METAL 710 710 Iron-sulfur (4Fe-4S).
 METAL 769 769 Iron-sulfur (4Fe-4S).
 METAL 772 772 Iron-sulfur (4Fe-4S).
 BINDING 191 191 Substrate.
 BINDING 498 498 Substrate.
 BINDING 791 791 Substrate.
 BINDING 796 796 Substrate.  
Keyword
 3D-structure; 4Fe-4S; Complete proteome; Direct protein sequencing; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome; Tricarboxylic acid cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 865 AA 
Protein Sequence
MLEEYRKHVA ERAAEGIAPK PLDANQMAAL VELLKNPPAG EEEFLLDLLT NRVPPGVDEA 60
AYVKAGFLAA IAKGEAKSPL LTPEKAIELL GTMQGGYNIH PLIDALDDAK LAPIAAKALS 120
HTLLMFDNFY DVEEKAKAGN EYAKQVMQSW ADAEWFLNRP ALAEKLTVTV FKVTGETNTD 180
DLSPAPDAWS RPDIPLHALA MLKNAREGIE PDQPGVVGPI KQIEALQQKG FPLAYVGDVV 240
GTGSSRKSAT NSVLWFMGDD IPHVPNKRGG GLCLGGKIAP IFFNTMEDAG ALPIEVDVSN 300
LNMGDVIDVY PYKGEVRNHE TGELLATFEL KTDVLIDEVR AGGRIPLIIG RGLTTKAREA 360
LGLPHSDVFR QAKDVAESDR GFSLAQKMVG RACGVKGIRP GAYCEPKMTS VGSQDTTGPM 420
TRDELKDLAC LGFSADLVMQ SFCHTAAYPK PVDVNTHHTL PDFIMNRGGV SLRPGDGVIH 480
SWLNRMLLPD TVGTGGDSHT RFPIGISFPA GSGLVAFAAA TGVMPLDMPE SVLVRFKGKM 540
QPGITLRDLV HAIPLYAIKQ GLLTVEKKGK KNIFSGRILE IEGLPDLKVE QAFELTDASA 600
ERSAAGCTIK LNKEPIIEYL NSNIVLLKWM IAEGYGDRRT LERRIQGMEK WLANPELLEA 660
DADAEYAAVI DIDLADIKEP ILCAPNDPDD ARPLSAVQGE KIDEVFIGSC MTNIGHFRAA 720
GKLLDAHKGQ LPTRLWVAPP TRMDAAQLTE EGYYSVFGKS GARIEIPGCS LCMGNQARVA 780
DGATVVSTST RNFPNRLGTG ANVFLASAEL AAVAALIGKL PTPEEYQTYV AQVDKTAVDT 840
YRYLNFNQLS QYTEKADGVI FQTAV 865 
Gene Ontology
 GO:0005829; C:cytosol; IEA:InterPro.
 GO:0047456; F:2-methylisocitrate dehydratase activity; IDA:EcoCyc.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
 GO:0003994; F:aconitate hydratase activity; IDA:EcoCyc.
 GO:0052632; F:citrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC.
 GO:0052633; F:isocitrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003730; F:mRNA 3'-UTR binding; IDA:EcoCyc.
 GO:0006097; P:glyoxylate cycle; NAS:EcoliWiki.
 GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IDA:EcoCyc.
 GO:0006417; P:regulation of translation; IDA:EcoCyc.
 GO:0006099; P:tricarboxylic acid cycle; NAS:EcoliWiki. 
Interpro
 IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
 IPR015937; Acoase/IPM_deHydtase.
 IPR001030; Acoase/IPM_deHydtase_lsu_aba.
 IPR015928; Aconitase/3IPM_dehydase_swvl.
 IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
 IPR018136; Aconitase_4Fe-4S_BS.
 IPR004406; Aconitase_B_bac.
 IPR015930; Aconitase_B_FeS-bd_bac.
 IPR015933; Aconitase_B_HEAT-like_bac.
 IPR015929; Aconitase_B_N_bac. 
Pfam
 PF00330; Aconitase
 PF06434; Aconitase_2_N
 PF11791; Aconitase_B_N 
SMART
  
PROSITE
 PS00450; ACONITASE_1
 PS01244; ACONITASE_2 
PRINTS