ACON_PIG
ID ACON_PIG Reviewed; 781 AA.
AC P16276;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Aconitate hydratase, mitochondrial;
DE Short=Aconitase;
DE EC=4.2.1.3 {ECO:0000269|PubMed:10631981};
DE AltName: Full=Citrate hydro-lyase;
DE Flags: Precursor;
GN Name=ACO2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, PYROGLUTAMATE
RP FORMATION AT GLN-28, AND SUBCELLULAR LOCATION.
RC TISSUE=Heart;
RX PubMed=2303429; DOI=10.1016/s0021-9258(19)39874-6;
RA Zheng L., Andrews P.C., Hermodson M.A., Dixon J.E., Zalkin H.;
RT "Cloning and structural characterization of porcine heart aconitase.";
RL J. Biol. Chem. 265:2814-2821(1990).
RN [2]
RP COFACTOR.
RX PubMed=27818104; DOI=10.1016/j.str.2016.08.020;
RA Cai K., Liu G., Frederick R.O., Xiao R., Montelione G.T., Markley J.L.;
RT "Structural/functional properties of human NFU1, an intermediate [4Fe-4S]
RT carrier in human mitochondrial iron-sulfur cluster biogenesis.";
RL Structure 24:2080-2091(2016).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 29-781 IN COMPLEX WITH
RP IRON-SULFUR, AND COFACTOR.
RC TISSUE=Heart;
RX PubMed=2726740; DOI=10.1073/pnas.86.10.3639;
RA Robbins A.H., Stout C.D.;
RT "Structure of activated aconitase: formation of the [4Fe-4S] cluster in the
RT crystal.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3639-3643(1989).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=2798408; DOI=10.1002/prot.340050406;
RA Robbins A.H., Stout C.D.;
RT "The structure of aconitase.";
RL Proteins 5:289-312(1989).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 29-779 OF MUTANT ALA-669 IN
RP COMPLEX WITH IRON-SULFUR; THE SUBSTRATE CITRATE AND ISOCITRATE, COFACTOR,
RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX PubMed=10631981; DOI=10.1110/ps.8.12.2655;
RA Lloyd S.J., Lauble H., Prasad G.S., Stout C.D.;
RT "The mechanism of aconitase: 1.8 A resolution crystal structure of the
RT S642A:citrate complex.";
RL Protein Sci. 8:2655-2662(1999).
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000269|PubMed:10631981}.
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:0000269|PubMed:10631981};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:10631981, ECO:0000269|PubMed:2726740,
CC ECO:0000269|PubMed:27818104};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. Binding of a [3Fe-4S]
CC cluster leads to an inactive enzyme. {ECO:0000269|PubMed:10631981,
CC ECO:0000269|PubMed:2726740};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10631981,
CC ECO:0000269|PubMed:2726740}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:2303429}.
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 -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; J05224; AAA30987.1; -; mRNA.
DR PIR; A35544; A35544.
DR RefSeq; NP_999119.1; NM_213954.1.
DR PDB; 1B0J; X-ray; 2.50 A; A=28-781.
DR PDB; 1B0K; X-ray; 2.50 A; A=29-781.
DR PDB; 1B0M; X-ray; 2.50 A; A=29-781.
DR PDB; 5ACN; X-ray; 2.10 A; A=29-781.
DR PDB; 6ACN; X-ray; 2.50 A; A=29-781.
DR PDB; 7ACN; X-ray; 2.00 A; A=29-781.
DR PDBsum; 1B0J; -.
DR PDBsum; 1B0K; -.
DR PDBsum; 1B0M; -.
DR PDBsum; 5ACN; -.
DR PDBsum; 6ACN; -.
DR PDBsum; 7ACN; -.
DR AlphaFoldDB; P16276; -.
DR SMR; P16276; -.
DR STRING; 9823.ENSSSCP00000000070; -.
DR CarbonylDB; P16276; -.
DR PaxDb; P16276; -.
DR PeptideAtlas; P16276; -.
DR PRIDE; P16276; -.
DR GeneID; 396999; -.
DR KEGG; ssc:396999; -.
DR CTD; 50; -.
DR eggNOG; KOG0453; Eukaryota.
DR InParanoid; P16276; -.
DR OrthoDB; 190960at2759; -.
DR BRENDA; 4.2.1.3; 6170.
DR UniPathway; UPA00223; UER00718.
DR EvolutionaryTrace; P16276; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0003994; F:aconitate hydratase activity; IBA:GO_Central.
DR GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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 3D-structure; 4Fe-4S; Acetylation; Direct protein sequencing; Iron;
KW Iron-sulfur; Lyase; Metal-binding; Mitochondrion; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT CHAIN 28..781
FT /note="Aconitate hydratase, mitochondrial"
FT /id="PRO_0000000543"
FT REGION 524..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10631981"
FT BINDING 192..194
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10631981"
FT BINDING 385
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:10631981,
FT ECO:0000269|PubMed:2726740"
FT BINDING 448
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:10631981,
FT ECO:0000269|PubMed:2726740"
FT BINDING 451
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:10631981,
FT ECO:0000269|PubMed:2726740"
FT BINDING 474
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10631981"
FT BINDING 479
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10631981"
FT BINDING 607
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10631981"
FT BINDING 670..671
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10631981"
FT MOD_RES 28
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2303429"
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 517
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 517
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 523
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KI0"
FT MOD_RES 523
FT /note="N6-succinyllysine; alternate"
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:0000250|UniProtKB:Q99798"
FT MOD_RES 573
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99798"
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:0000250|UniProtKB:Q99798"
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 STRAND 33..35
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:1B0J"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:7ACN"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:7ACN"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:7ACN"
FT TURN 257..262
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 277..286
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 361..371
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:7ACN"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 390..404
FT /evidence="ECO:0007829|PDB:7ACN"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 421..429
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 432..438
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 449..452
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 466..473
FT /evidence="ECO:0007829|PDB:7ACN"
FT TURN 477..481
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 493..502
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:7ACN"
FT TURN 509..511
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:1B0J"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:1B0J"
FT TURN 549..551
FT /evidence="ECO:0007829|PDB:1B0M"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 579..588
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 594..597
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 601..606
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 610..613
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:7ACN"
FT TURN 617..620
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:7ACN"
FT TURN 624..627
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:6ACN"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 643..652
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 657..660
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:6ACN"
FT HELIX 673..680
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 683..689
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 693..701
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 705..711
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 712..717
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 723..727
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 729..731
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 738..743
FT /evidence="ECO:0007829|PDB:7ACN"
FT STRAND 749..755
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 760..768
FT /evidence="ECO:0007829|PDB:7ACN"
FT HELIX 771..778
FT /evidence="ECO:0007829|PDB:7ACN"
SQ SEQUENCE 781 AA; 85761 MW; 5737FD9BCFCEF184 CRC64;
MAPYSLLVTR LQKALGVRQY HVASVLCQRA KVAMSHFEPH EYIRYDLLEK NIDIVRKRLN
RPLTLSEKIV YGHLDDPANQ EIERGKTYLR LRPDRVAMQD ATAQMAMLQF ISSGLPKVAV
PSTIHCDHLI EAQLGGEKDL RRAKDINQEV YNFLATAGAK YGVGFWRPGS GIIHQIILEN
YAYPGVLLIG TDSHTPNGGG LGGICIGVGG ADAVDVMAGI PWELKCPKVI GVKLTGSLSG
WTSPKDVILK VAGILTVKGG TGAIVEYHGP GVDSISCTGM ATICNMGAEI GATTSVFPYN
HRMKKYLSKT GRADIANLAD EFKDHLVPDP GCHYDQVIEI NLSELKPHIN GPFTPDLAHP
VAEVGSVAEK EGWPLDIRVG LIGSCTNSSY EDMGRSAAVA KQALAHGLKC KSQFTITPGS
EQIRATIERD GYAQVLRDVG GIVLANACGP CIGQWDRKDI KKGEKNTIVT SYNRNFTGRN
DANPETHAFV TSPEIVTALA IAGTLKFNPE TDFLTGKDGK KFKLEAPDAD ELPRAEFDPG
QDTYQHPPKD SSGQRVDVSP TSQRLQLLEP FDKWDGKDLE DLQILIKVKG KCTTDHISAA
GPWLKFRGHL DNISNNLLIG AINIENRKAN SVRNAVTQEF GPVPDTARYY KQHGIRWVVI
GDENYGEGSS REHRALEPRH LGGRAIITKS FARIHETNLK KQGLLPLTFA DPADYNKIHP
VDKLTIQGLK DFAPGKPLKC IIKHPNGTQE TILLNHTFNE TQIEWFRAGS ALNRMKELQQ
K
