ID   ACON_GRAGA              Reviewed;         779 AA.
AC   P49609;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Aconitate hydratase, mitochondrial;
DE            Short=Aconitase;
DE            EC=4.2.1.3;
DE   AltName: Full=Citrate hydro-lyase;
DE   Flags: Precursor;
OS   Gracilaria gracilis (Red alga).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC   Gracilariaceae; Gracilaria.
OX   NCBI_TaxID=2777;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7647296; DOI=10.1007/bf00021189;
RA   Zhou Y.H., Ragan M.A.;
RT   "Characterization of the nuclear gene encoding mitochondrial aconitase in
RT   the marine red alga Gracilaria verrucosa.";
RL   Plant Mol. Biol. 28:635-646(1995).
CC   -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC       aconitate. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 2/2.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; U17709; AAA80494.1; -; Genomic_DNA.
DR   PIR; S57805; S57805.
DR   AlphaFoldDB; P49609; -.
DR   SMR; P49609; -.
DR   UniPathway; UPA00223; UER00718.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Mitochondrion;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..28
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..779
FT                   /note="Aconitate hydratase, mitochondrial"
FT                   /id="PRO_0000000548"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         190..192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         383
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         446
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         449
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         472
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         477
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         605
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         668..669
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   779 AA;  83731 MW;  962173FFA8CBB836 CRC64;
     MIAMDRIARI PIARWTSRAF RVSAAARQTP MSPLEAHNEL EPVYAAIDDR LNTVRSKLNR
     PLTLAEKVLY GHLDDPERVP VRGETFLKLR PERVALQDAT AQMALIQFMA SARPQVAVPS
     TIHCDHLIAA EVGAEEDMAK AKSQNKEVYD FLASAGAKYG LGFWKPGSGI IHQIVLENYA
     FPGLLMIGTD SHTPNAGGLG ACAVGVGGAD AVDVMVGLPW ELKAPKVIGV KLTGKLQEWA
     SPKDVILKVA GILTVKGGTG AIVEYFGEGV DSLSCTGMGT ICNMGAEIGA TTSMFPYNSR
     MGDYLKATGR DGIASLADSF SEQLRADENA VYDQLIEINL SELEPHINGP FTPDLAHPLS
     KFKEEVEKNG WPAELTVGLI GSCTNSSYED MARSASVVKQ ALSHGVKSKS IFNITPGSEQ
     VRATISRDGI LDTFTEAGGT VLANACGPCI GQWNRSDVPK GTPNSIITSF NRNFSQRNDG
     NPQTHAFVAS PEIVTAMSLA GSLKFNPATD SLQGADGAEF KLAAPSGDEL PVMGFDPGED
     TFQPPSDDST SILVQIDPDS QRLSFLEPFP AWDGKDYTDM PVLIKARGKC TTDHISMAGP
     WLKFRGHLDN ISNNMLIGAV NDENGEINNV KNAVTGEYGT VPDTARAYKA EGVKWVVIGD
     ENYGEGSSRE HAALEPRHLG GVAVIVKSFA RIHETNLKKQ GMLPLTFNNP ADYDKIDSSD
     KVSLVGLKNL TPGEPVTMTV TKADGTSMDI LLNHTFNDEQ LEWFRAGSAL NKIKIDLGT