UniProt Accession

 ACON_MOUSE; Q99KI0; Q3UDK9; Q3ULG9; Q3UNH7; Q505P4 

Genbank Protein ID

 AK143917; AK144207; AK145511; AK150027; AK165411; BC004645; BC094462 

Genbank Nucleotide ID

 BAE25602.1; BAE25770.1; BAE26479.1; BAE29252.1; BAE38169.1; AAH04645.1; AAH94462.1 

Protein Name

 Aconitate hydratase, mitochondrial 

Protein Synonyms/Alias

 Aconitase; Citrate hydro-lyase 

Gene Name

 Aco2 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
31	SVLCQRAKVAMSHFE	acetylation	[1, 2]
31	SVLCQRAKVAMSHFE	succinylation	[2]
31	SVLCQRAKVAMSHFE	ubiquitination	[3]
50	IRYDLLEKNINIVRK	acetylation	[1, 2, 4, 5, 6, 7, 8, 9, 10, 11, 12]
50	IRYDLLEKNINIVRK	succinylation	[2]
50	IRYDLLEKNINIVRK	ubiquitination	[3]
138	EAQVGGEKDLRRAKD	acetylation	[1, 2, 11, 12]
138	EAQVGGEKDLRRAKD	succinylation	[2]
144	EKDLRRAKDINQEVY	acetylation	[1, 2, 7, 8, 11, 12]
144	EKDLRRAKDINQEVY	succinylation	[2]
144	EKDLRRAKDINQEVY	succinylation	[2]
144	EKDLRRAKDINQEVY	ubiquitination	[3, 13]
225	AGIPWELKCPKVIGV	acetylation	[7]
228	PWELKCPKVIGVKLT	acetylation	[2, 7, 11]
228	PWELKCPKVIGVKLT	succinylation	[2]
233	CPKVIGVKLTGSLSG	acetylation	[2, 7, 11]
233	CPKVIGVKLTGSLSG	succinylation	[2]
245	LSGWTSPKDVILKVA	acetylation	[8]
401	GRSAAVAKQALAHGL	acetylation	[1, 2, 7]
401	GRSAAVAKQALAHGL	succinylation	[2]
401	GRSAAVAKQALAHGL	ubiquitination	[3]
409	QALAHGLKCKSQFTI	acetylation	[1, 11]
411	LAHGLKCKSQFTITP	acetylation	[1, 2, 7, 12]
411	LAHGLKCKSQFTITP	succinylation	[2]
465	KDIKKGEKNTIVTSY	acetylation	[1, 12]
517	ETDFLTGKDGKKFKL	acetylation	[1, 2, 7, 9, 11, 12]
517	ETDFLTGKDGKKFKL	succinylation	[2]
517	ETDFLTGKDGKKFKL	ubiquitination	[3]
520	FLTGKDGKKFKLEAP	acetylation	[1]
521	LTGKDGKKFKLEAPD	acetylation	[1, 7, 10]
523	GKDGKKFKLEAPDAD	acetylation	[1, 2, 5, 7, 8, 9, 11, 12]
523	GKDGKKFKLEAPDAD	succinylation	[2]
549	DTYQHPPKDSSGQRV	acetylation	[1, 2, 11]
549	DTYQHPPKDSSGQRV	succinylation	[2]
549	DTYQHPPKDSSGQRV	ubiquitination	[3]
573	QLLEPFDKWDGKDLE	acetylation	[1, 2, 7, 12]
573	QLLEPFDKWDGKDLE	succinylation	[2]
573	QLLEPFDKWDGKDLE	ubiquitination	[3]
577	PFDKWDGKDLEDLQI	acetylation	[2, 7]
577	PFDKWDGKDLEDLQI	succinylation	[2]
591	ILIKVKGKCTTDHIS	acetylation	[2, 11]
591	ILIKVKGKCTTDHIS	succinylation	[2]
605	SAAGPWLKFRGHLDN	acetylation	[1, 2, 5, 11, 12]
605	SAAGPWLKFRGHLDN	succinylation	[2]
628	AINIENGKANSVRNA	acetylation	[2, 11, 12]
628	AINIENGKANSVRNA	succinylation	[2]
689	GGRAIITKSFARIHE	acetylation	[1, 2, 5, 8, 11, 12]
689	GGRAIITKSFARIHE	succinylation	[2]
700	RIHETNLKKQGLLPL	acetylation	[11, 12]
701	IHETNLKKQGLLPLT	acetylation	[8]
701	IHETNLKKQGLLPLT	ubiquitination	[3]
717	ADPSDYNKIHPVDKL	acetylation	[12]
723	NKIHPVDKLTIQGLK	acetylation	[1, 2, 7, 11, 12]
723	NKIHPVDKLTIQGLK	succinylation	[2]
723	NKIHPVDKLTIQGLK	ubiquitination	[3]
730	KLTIQGLKDFAPGKP	acetylation	[1, 2, 7, 8, 11, 12]
730	KLTIQGLKDFAPGKP	succinylation	[2]
736	LKDFAPGKPLKCVIK	acetylation	[1, 2, 7, 8, 11, 12]
736	LKDFAPGKPLKCVIK	succinylation	[2]
736	LKDFAPGKPLKCVIK	succinylation	[2]
736	LKDFAPGKPLKCVIK	ubiquitination	[3]
739	FAPGKPLKCVIKHPN	acetylation	[1, 7, 11, 12]
743	KPLKCVIKHPNGTQE	acetylation	[1, 10, 11, 12]

Reference

 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [4] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [5] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [6] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [7] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [8] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [9] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [10] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [11] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [12] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [13] A proteomics approach to identify the ubiquitinated proteins in mouse heart.
 Jeon HB, Choi ES, Yoon JH, Hwang JH, Chang JW, Lee EK, Choi HW, Park ZY, Yoo YJ.
 Biochem Biophys Res Commun. 2007 Jun 8;357(3):731-6. [PMID: 17451654] 

Functional Description

 Catalyzes the isomerization of citrate to isocitrate via cis-aconitate (By similarity). 

Sequence Annotation

 REGION 192 194 Substrate binding (By similarity).
 REGION 670 671 Substrate binding (By similarity).
 METAL 385 385 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 448 448 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 451 451 Iron-sulfur (4Fe-4S) (By similarity).
 BINDING 99 99 Substrate (By similarity).
 BINDING 474 474 Substrate (By similarity).
 BINDING 479 479 Substrate (By similarity).
 BINDING 607 607 Substrate (By similarity).
 MOD_RES 28 28 Pyrrolidone carboxylic acid (By
 MOD_RES 50 50 N6-acetyllysine.
 MOD_RES 559 559 Phosphoserine (By similarity).
 MOD_RES 573 573 N6-acetyllysine (By similarity).
 MOD_RES 605 605 N6-acetyllysine (By similarity).
 CROSSLNK 144 144 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 4Fe-4S; Acetylation; Complete proteome; Direct protein sequencing; Iron; Iron-sulfur; Isopeptide bond; Lyase; Metal-binding; Mitochondrion; Phosphoprotein; Pyrrolidone carboxylic acid; Reference proteome; Transit peptide; Tricarboxylic acid cycle; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 780 AA 

Protein Sequence

Gene Ontology

 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:Compara.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0003994; F:aconitate hydratase activity; IDA:MGI.
 GO:0052632; F:citrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC.
 GO:0005506; F:iron ion binding; IEA:Compara.
 GO:0052633; F:isocitrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC.
 GO:0006101; P:citrate metabolic process; IEA:Compara.
 GO:0006102; P:isocitrate metabolic process; IEA:Compara.
 GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. 

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.
 IPR006248; Aconitase_mito-like.
 IPR000573; AconitaseA/IPMdHydase_ssu_swvl. 

Pfam

 PF00330; Aconitase
 PF00694; Aconitase_C 

SMART

  

PROSITE

 PS00450; ACONITASE_1
 PS01244; ACONITASE_2 

PRINTS

 PR00415; ACONITASE.