ACON_HUMAN
ID ACON_HUMAN Reviewed; 780 AA.
AC Q99798; O75809; Q5JZ41; Q6FHX0; Q8TAQ6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Aconitate hydratase, mitochondrial;
DE Short=Aconitase;
DE EC=4.2.1.3 {ECO:0000250|UniProtKB:P16276};
DE AltName: Full=Citrate hydro-lyase;
DE Flags: Precursor;
GN Name=ACO2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RA Juang H.H., Chiou B.;
RT "Cloning and structural characterization of human mitochondrial
RT aconitase.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9630632; DOI=10.1016/s0378-1119(98)00188-7;
RA Mirel D.B., Marder K., Graziano J., Freyer G., Zhao Q., Mayeux R.,
RA Wilhelmsen K.C.;
RT "Characterization of the human mitochondrial aconitase gene (ACO2).";
RL Gene 213:205-218(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 69-84; 234-245; 313-323; 379-395; 412-424; 430-437;
RP 507-520; 565-573; 608-628; 634-648 AND 657-671, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 69-83; 96-107; 371-396 AND 524-534.
RX PubMed=1946331;
RA Baldwin G.S., Seet K.L., Callaghan J., Toncich G., Toh B.H., Moritz R.L.,
RA Rubira M.R., Simpson R.;
RT "Purification and partial amino acid sequence of human aconitase.";
RL Protein Seq. Data Anal. 4:63-67(1991).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-573 AND LYS-605, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP INVOLVEMENT IN OPA9, INVOLVEMENT IN ICRD, VARIANTS OPA9 VAL-74 AND ARG-661,
RP AND VARIANTS ICRD ASP-259 AND ASN-736.
RX PubMed=25351951; DOI=10.1136/jmedgenet-2014-102532;
RA Metodiev M.D., Gerber S., Hubert L., Delahodde A., Chretien D., Gerard X.,
RA Amati-Bonneau P., Giacomotto M.C., Boddaert N., Kaminska A., Desguerre I.,
RA Amiel J., Rio M., Kaplan J., Munnich A., Rotig A., Rozet J.M., Besmond C.;
RT "Mutations in the tricarboxylic acid cycle enzyme, aconitase 2, cause
RT either isolated or syndromic optic neuropathy with encephalopathy and
RT cerebellar atrophy.";
RL J. Med. Genet. 51:834-838(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-697.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [17]
RP VARIANT ICRD ARG-112, AND CHARACTERIZATION OF VARIANT ICRD ARG-112.
RX PubMed=22405087; DOI=10.1016/j.ajhg.2012.01.009;
RA Spiegel R., Pines O., Ta-Shma A., Burak E., Shaag A., Halvardson J.,
RA Edvardson S., Mahajna M., Zenvirt S., Saada A., Shalev S., Feuk L.,
RA Elpeleg O.;
RT "Infantile cerebellar-retinal degeneration associated with a mutation in
RT mitochondrial aconitase, ACO2.";
RL Am. J. Hum. Genet. 90:518-523(2012).
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000250|UniProtKB:P16276}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:P16276};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P16276};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. Binding of a [3Fe-4S]
CC cluster leads to an inactive enzyme. {ECO:0000250|UniProtKB:P16276};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P16276}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P16276}.
CC -!- PTM: Forms covalent cross-links mediated by transglutaminase TGM2,
CC between a glutamine and the epsilon-amino group of a lysine residue,
CC forming homopolymers and heteropolymers.
CC {ECO:0000250|UniProtKB:Q9ER34}.
CC -!- DISEASE: Infantile cerebellar-retinal degeneration (ICRD) [MIM:614559]:
CC A severe autosomal recessive neurodegenerative disorder characterized
CC by onset between ages 2 and 6 months of truncal hypotonia, athetosis,
CC seizures, and ophthalmologic abnormalities, particularly optic atrophy
CC and retinal degeneration. Affected individuals show profound
CC psychomotor retardation, with only some achieving rolling, sitting, or
CC recognition of family. Brain MRI shows progressive cerebral and
CC cerebellar degeneration. {ECO:0000269|PubMed:22405087,
CC ECO:0000269|PubMed:25351951}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Optic atrophy 9 (OPA9) [MIM:616289]: A condition that features
CC progressive visual loss in association with optic atrophy. Atrophy of
CC the optic disk indicates a deficiency in the number of nerve fibers
CC which arise in the retina and converge to form the optic disk, optic
CC nerve, optic chiasm and optic tracts. {ECO:0000269|PubMed:25351951}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Aconitase entry;
CC URL="https://en.wikipedia.org/wiki/Aconitase";
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DR EMBL; U80040; AAB38416.1; -; mRNA.
DR EMBL; U87939; AAC39921.1; -; Genomic_DNA.
DR EMBL; U87926; AAC39921.1; JOINED; Genomic_DNA.
DR EMBL; U87927; AAC39921.1; JOINED; Genomic_DNA.
DR EMBL; U87928; AAC39921.1; JOINED; Genomic_DNA.
DR EMBL; U87929; AAC39921.1; JOINED; Genomic_DNA.
DR EMBL; U87930; AAC39921.1; JOINED; Genomic_DNA.
DR EMBL; U87931; AAC39921.1; JOINED; Genomic_DNA.
DR EMBL; U87932; AAC39921.1; JOINED; Genomic_DNA.
DR EMBL; U87933; AAC39921.1; JOINED; Genomic_DNA.
DR EMBL; U87934; AAC39921.1; JOINED; Genomic_DNA.
DR EMBL; U87935; AAC39921.1; JOINED; Genomic_DNA.
DR EMBL; U87936; AAC39921.1; JOINED; Genomic_DNA.
DR EMBL; U87937; AAC39921.1; JOINED; Genomic_DNA.
DR EMBL; U87938; AAC39921.1; JOINED; Genomic_DNA.
DR EMBL; CR456365; CAG30251.1; -; mRNA.
DR EMBL; CR536568; CAG38805.1; -; mRNA.
DR EMBL; AL023553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL008582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014092; AAH14092.1; -; mRNA.
DR EMBL; BC026196; AAH26196.1; -; mRNA.
DR CCDS; CCDS14017.1; -.
DR PIR; S17526; S17526.
DR PIR; T52543; T52543.
DR RefSeq; NP_001089.1; NM_001098.2.
DR AlphaFoldDB; Q99798; -.
DR SMR; Q99798; -.
DR BioGRID; 106566; 183.
DR IntAct; Q99798; 14.
DR MINT; Q99798; -.
DR STRING; 9606.ENSP00000216254; -.
DR DrugBank; DB03964; 4-Hydroxy-Aconitate Ion.
DR DrugBank; DB04351; Aconitate Ion.
DR DrugBank; DB04072; Alpha-Methylisocitric Acid.
DR DrugBank; DB01727; Isocitric Acid.
DR DrugBank; DB04562; Tricarballylic acid.
DR CarbonylDB; Q99798; -.
DR GlyGen; Q99798; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99798; -.
DR PhosphoSitePlus; Q99798; -.
DR SwissPalm; Q99798; -.
DR BioMuta; ACO2; -.
DR DMDM; 6686275; -.
DR DOSAC-COBS-2DPAGE; Q99798; -.
DR REPRODUCTION-2DPAGE; IPI00017855; -.
DR REPRODUCTION-2DPAGE; Q99798; -.
DR SWISS-2DPAGE; Q99798; -.
DR UCD-2DPAGE; Q99798; -.
DR EPD; Q99798; -.
DR jPOST; Q99798; -.
DR MassIVE; Q99798; -.
DR MaxQB; Q99798; -.
DR PaxDb; Q99798; -.
DR PeptideAtlas; Q99798; -.
DR PRIDE; Q99798; -.
DR ProteomicsDB; 78478; -.
DR Antibodypedia; 240; 527 antibodies from 39 providers.
DR DNASU; 50; -.
DR Ensembl; ENST00000216254.9; ENSP00000216254.4; ENSG00000100412.17.
DR GeneID; 50; -.
DR KEGG; hsa:50; -.
DR MANE-Select; ENST00000216254.9; ENSP00000216254.4; NM_001098.3; NP_001089.1.
DR UCSC; uc003bac.3; human.
DR CTD; 50; -.
DR DisGeNET; 50; -.
DR GeneCards; ACO2; -.
DR HGNC; HGNC:118; ACO2.
DR HPA; ENSG00000100412; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR MalaCards; ACO2; -.
DR MIM; 100850; gene.
DR MIM; 614559; phenotype.
DR MIM; 616289; phenotype.
DR neXtProt; NX_Q99798; -.
DR OpenTargets; ENSG00000100412; -.
DR Orphanet; 98676; Autosomal recessive isolated optic atrophy.
DR Orphanet; 313850; Infantile cerebellar-retinal degeneration.
DR PharmGKB; PA24443; -.
DR VEuPathDB; HostDB:ENSG00000100412; -.
DR eggNOG; KOG0453; Eukaryota.
DR GeneTree; ENSGT00940000154892; -.
DR HOGENOM; CLU_006714_2_2_1; -.
DR InParanoid; Q99798; -.
DR OrthoDB; 190960at2759; -.
DR PhylomeDB; Q99798; -.
DR TreeFam; TF300627; -.
DR BioCyc; MetaCyc:HS02077-MON; -.
DR BRENDA; 4.2.1.3; 2681.
DR PathwayCommons; Q99798; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
DR SignaLink; Q99798; -.
DR SIGNOR; Q99798; -.
DR UniPathway; UPA00223; UER00718.
DR BioGRID-ORCS; 50; 385 hits in 1091 CRISPR screens.
DR ChiTaRS; ACO2; human.
DR GenomeRNAi; 50; -.
DR Pharos; Q99798; Tbio.
DR PRO; PR:Q99798; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q99798; protein.
DR Bgee; ENSG00000100412; Expressed in heart right ventricle and 199 other tissues.
DR ExpressionAtlas; Q99798; baseline and differential.
DR Genevisible; Q99798; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:Ensembl.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0003994; F:aconitate hydratase activity; EXP:Reactome.
DR GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IDA:MGI.
DR GO; GO:0006101; P:citrate metabolic process; IDA:MGI.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
DR GO; GO:0006102; P:isocitrate metabolic process; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0035900; P:response to isolation stress; IEA:Ensembl.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:MGI.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR Gene3D; 3.40.1060.10; -; 1.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR015932; Aconitase_dom2.
DR InterPro; IPR006248; Aconitase_mito-like.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR01340; aconitase_mito; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Acetylation; Direct protein sequencing; Disease variant; Iron;
KW Iron-sulfur; Lyase; Metal-binding; Mitochondrion; Neurodegeneration;
KW Phosphoprotein; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 28..780
FT /note="Aconitate hydratase, mitochondrial"
FT /id="PRO_0000000541"
FT REGION 528..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 192..194
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 451
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 474
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 607
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 670..671
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 31
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 50
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 50
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 138
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 138
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 144
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 144
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 233
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 233
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 411
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 549
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 573
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 573
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 577
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 591
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 605
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 605
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 628
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 689
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 723
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 723
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 730
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 730
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 736
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 739
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 743
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT VARIANT 74
FT /note="L -> V (in OPA9; dbSNP:rs141772938)"
FT /evidence="ECO:0000269|PubMed:25351951"
FT /id="VAR_073435"
FT VARIANT 112
FT /note="S -> R (in ICRD; functional expression studies in
FT yeast show that the mutant has decreased function under
FT growth conditions requiring the TCA cycle and the
FT glyoxylate shunt; dbSNP:rs786200924)"
FT /evidence="ECO:0000269|PubMed:22405087"
FT /id="VAR_067543"
FT VARIANT 259
FT /note="G -> D (in ICRD; dbSNP:rs786204828)"
FT /evidence="ECO:0000269|PubMed:25351951"
FT /id="VAR_073436"
FT VARIANT 661
FT /note="G -> R (in OPA9; dbSNP:rs752034900)"
FT /evidence="ECO:0000269|PubMed:25351951"
FT /id="VAR_073437"
FT VARIANT 697
FT /note="T -> N (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036572"
FT VARIANT 736
FT /note="K -> N (in ICRD; dbSNP:rs786204829)"
FT /evidence="ECO:0000269|PubMed:25351951"
FT /id="VAR_073438"
FT VARIANT 768
FT /note="A -> S (in dbSNP:rs1804785)"
FT /id="VAR_033297"
FT CONFLICT 35
FT /note="S -> T (in Ref. 1; AAB38416)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="G -> D (in Ref. 1; AAB38416)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="A -> D (in Ref. 1; AAB38416)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="K -> S (in Ref. 1; AAB38416)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="G -> D (in Ref. 4; CAG38805)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="G -> R (in Ref. 6; AAH26196)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="S -> T (in Ref. 1; AAB38416)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="P -> H (in Ref. 6; AAH26196)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="I -> M (in Ref. 1; AAB38416)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="L -> P (in Ref. 4; CAG38805)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="T -> K (in Ref. 1; AAB38416)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="G -> R (in Ref. 1; AAB38416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 780 AA; 85425 MW; 58C9FFBDBDC63D5E CRC64;
MAPYSLLVTR LQKALGVRQY HVASVLCQRA KVAMSHFEPN EYIHYDLLEK NINIVRKRLN
RPLTLSEKIV YGHLDDPASQ EIERGKSYLR LRPDRVAMQD ATAQMAMLQF ISSGLSKVAV
PSTIHCDHLI EAQVGGEKDL RRAKDINQEV YNFLATAGAK YGVGFWKPGS GIIHQIILEN
YAYPGVLLIG TDSHTPNGGG LGGICIGVGG ADAVDVMAGI PWELKCPKVI GVKLTGSLSG
WSSPKDVILK VAGILTVKGG TGAIVEYHGP GVDSISCTGM ATICNMGAEI GATTSVFPYN
HRMKKYLSKT GREDIANLAD EFKDHLVPDP GCHYDQLIEI NLSELKPHIN GPFTPDLAHP
VAEVGKVAEK EGWPLDIRVG LIGSCTNSSY EDMGRSAAVA KQALAHGLKC KSQFTITPGS
EQIRATIERD GYAQILRDLG GIVLANACGP CIGQWDRKDI KKGEKNTIVT SYNRNFTGRN
DANPETHAFV TSPEIVTALA IAGTLKFNPE TDYLTGTDGK KFRLEAPDAD ELPKGEFDPG
QDTYQHPPKD SSGQHVDVSP TSQRLQLLEP FDKWDGKDLE DLQILIKVKG KCTTDHISAA
GPWLKFRGHL DNISNNLLIG AINIENGKAN SVRNAVTQEF GPVPDTARYY KKHGIRWVVI
GDENYGEGSS REHAALEPRH LGGRAIITKS FARIHETNLK KQGLLPLTFA DPADYNKIHP
VDKLTIQGLK DFTPGKPLKC IIKHPNGTQE TILLNHTFNE TQIEWFRAGS ALNRMKELQQ
