ID   ACOHC_SOLTU             Reviewed;         616 AA.
AC   O04916;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Aconitate hydratase, cytoplasmic;
DE            Short=Aconitase;
DE            EC=4.2.1.3;
DE   AltName: Full=Citrate hydro-lyase;
DE   Flags: Fragment;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Desiree;
RA   Surpili M.J.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
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; glyoxylate and dicarboxylate
CC       metabolism.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; X97012; CAA65735.1; -; mRNA.
DR   PIR; T07611; T07611.
DR   AlphaFoldDB; O04916; -.
DR   SMR; O04916; -.
DR   STRING; 4113.PGSC0003DMT400074489; -.
DR   eggNOG; KOG0452; Eukaryota.
DR   UniPathway; UPA00227; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; O04916; baseline.
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:0030350; F:iron-responsive element binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006101; P:citrate metabolic process; IBA:GO_Central.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   CDD; cd01580; AcnA_IRP_Swivel; 1.
DR   Gene3D; 3.20.19.10; -; 1.
DR   Gene3D; 3.30.499.10; -; 2.
DR   InterPro; IPR044137; AcnA_IRP_Swivel.
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; IPR006249; Aconitase/IRP2.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   PANTHER; PTHR11670; PTHR11670; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   TIGRFAMs; TIGR01341; aconitase_1; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Cytoplasm; Glyoxylate bypass; Iron; Iron-sulfur; Lyase;
KW   Metal-binding; Reference proteome.
FT   CHAIN           <1..616
FT                   /note="Aconitate hydratase, cytoplasmic"
FT                   /id="PRO_0000076654"
FT   BINDING         159
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         421
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         502..503
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   616 AA;  67161 MW;  7563871E3F353521 CRC64;
     EFYGGGMSGL SLADRATIAN MAPEYGATMG FFPVDHVTLE YLKLTGRSDE IVGMVEAYLR
     ANNMFVDYNE PQQEKVYSSY LNLDLADVEP CLSGPKRPHD RVPLKEMKSD WHALLDNKVG
     FKGFAVPKEV QDKVAKFSFH GQPAELKHGS VVIAAITSCT NTSNPSVMLG AALVAKKASE
     LGLHVKPWVK TSLAPGSGVV TKYLLKSGLQ KYLNQQGFNI VGYGCTTCIG NSGDLDESVA
     SAISENDIVA AAVLSGNRNF EGRVHALTRA NYLASPPLVV AYALAGTVDI DFEKDPIGVG
     KDGKDVYFRD IWPSTEEIAE VVQSSVLPDM FKSTYEAITK GNTMWNELSV PTTKLYQWDP
     KSTYIHEPPY FKGMTMDPPG PHGVKDAYCL LNFGDSITTD HISPAGSIHK DSPAARYLME
     RGVDRRDFNS YGSRRGNDEI MARGTFANIR LVNKLLNGEV GPKTVHVPSG EKLSVFDAAM
     KYKSAGQSTI ILAGAEYGSG SSRDWAAKGP MLLGVKAVIA KSFERIHRSN LVGMGIVPLC
     FKAGEDADTL GLTGQERYTI DLPENISEIR PGQDVTVQTD TGKSFTCIVR FDTEVELAYF
     NHGGILQYVI RQLTQR