CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005407
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aconitate hydratase 1 
Protein Synonyms/Alias
 Aconitase 1; Citrate hydro-lyase 1 
Gene Name
 acnA 
Gene Synonyms/Alias
 acn; b1276; JW1268 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
18DTLQAKDKTYHYYSLacetylation[1, 2]
30YSLPLAAKSLGDITRacetylation[2]
71HALAGWLKNAHADREacetylation[1]
161HERYVFLKWGKQAFSacetylation[2]
164YVFLKWGKQAFSRFSacetylation[2]
283RKHGVVGKFVEFYGDacetylation[2]
342DQVELVEKYAKAQGMacetylation[2]
391VALPDVPKAFAASNEacetylation[1, 2]
460KAVTLGLKRQPWVKAacetylation[2]
482VVSDYLAKAKLTPYLacetylation[1, 2]
585KGDPVYLKDIWPSAQacetylation[2]
684ISPAGSIKPDSPAGRacetylation[1, 2]
758YDAAMRYKQEQTPLAacetylation[1]
770PLAVIAGKEYGSGSSacetylation[2]
832LGLTGEEKIDIGDLQacetylation[2]
Reference
 [1] 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]
 [2] 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
Functional Description
 Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. May have an iron-responsive regulatory function. 
Sequence Annotation
 METAL 435 435 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 501 501 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 504 504 Iron-sulfur (4Fe-4S) (By similarity).  
Keyword
 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
 891 AA 
Protein Sequence
MSSTLREASK DTLQAKDKTY HYYSLPLAAK SLGDITRLPK SLKVLLENLL RWQDGNSVTE 60
EDIHALAGWL KNAHADREIA YRPARVLMQD FTGVPAVVDL AAMREAVKRL GGDTAKVNPL 120
SPVDLVIDHS VTVDRFGDDE AFEENVRLEM ERNHERYVFL KWGKQAFSRF SVVPPGTGIC 180
HQVNLEYLGK AVWSELQDGE WIAYPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ 240
PVSMLIPDVV GFKLTGKLRE GITATDLVLT VTQMLRKHGV VGKFVEFYGD GLDSLPLADR 300
ATIANMSPEY GATCGFFPID AVTLDYMRLS GRSEDQVELV EKYAKAQGMW RNPGDEPIFT 360
STLELDMNDV EASLAGPKRP QDRVALPDVP KAFAASNELE VNATHKDRQP VDYVMNGHQY 420
QLPDGAVVIA AITSCTNTSN PSVLMAAGLL AKKAVTLGLK RQPWVKASLA PGSKVVSDYL 480
AKAKLTPYLD ELGFNLVGYG CTTCIGNSGP LPDPIETAIK KSDLTVGAVL SGNRNFEGRI 540
HPLVKTNWLA SPPLVVAYAL AGNMNINLAS EPIGHDRKGD PVYLKDIWPS AQEIARAVEQ 600
VSTEMFRKEY AEVFEGTAEW KGINVTRSDT YGWQEDSTYI RLSPFFDEMQ ATPAPVEDIH 660
GARILAMLGD SVTTDHISPA GSIKPDSPAG RYLQGRGVER KDFNSYGSRR GNHEVMMRGT 720
FANIRIRNEM VPGVEGGMTR HLPDSDVVSI YDAAMRYKQE QTPLAVIAGK EYGSGSSRDW 780
AAKGPRLLGI RVVIAESFER IHRSNLIGMG ILPLEFPQGV TRKTLGLTGE EKIDIGDLQN 840
LQPGATVPVT LTRADGSQEV VPCRCRIDTA TELTYYQNDG ILHYVIRNML K 891 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:EcoliWiki.
 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:0005506; F:iron ion binding; IMP:EcoliWiki.
 GO:0052633; F:isocitrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC.
 GO:0003730; F:mRNA 3'-UTR binding; IDA:EcoCyc.
 GO:0009061; P:anaerobic respiration; IDA:EcoliWiki.
 GO:0006097; P:glyoxylate cycle; NAS:EcoliWiki.
 GO:0006979; P:response to oxidative stress; IDA:EcoliWiki.
 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.
 IPR006249; Aconitase/Fe_reg_prot_2.
 IPR015934; Aconitase/Fe_reg_prot_2/AcnD.
 IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
 IPR018136; Aconitase_4Fe-4S_BS.
 IPR000573; AconitaseA/IPMdHydase_ssu_swvl. 
Pfam
 PF00330; Aconitase
 PF00694; Aconitase_C 
SMART
  
PROSITE
 PS00450; ACONITASE_1
 PS01244; ACONITASE_2 
PRINTS
 PR00415; ACONITASE.