ID   ACOHC_CUCMC             Reviewed;         764 AA.
AC   Q42669;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Aconitate hydratase;
DE            Short=Aconitase;
DE            EC=4.2.1.3;
DE   AltName: Full=Citrate hydro-lyase;
DE   Flags: Fragment;
GN   Name=ACO;
OS   Cucumis melo var. conomon (Oriental pickling melon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3657;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Cantaloupe; TISSUE=Fruit;
RX   PubMed=7713917; DOI=10.1074/jbc.270.14.8131;
RA   Peyret P., Perez P., Alric M.;
RT   "Structure, genomic organization, and expression of the Arabidopsis
RT   thaliana aconitase gene. Plant aconitase show significant homology with
RT   mammalian iron-responsive element-binding protein.";
RL   J. Biol. Chem. 270:8131-8137(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; 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; X82840; CAA58047.1; -; mRNA.
DR   PIR; S49849; S49849.
DR   AlphaFoldDB; Q42669; -.
DR   SMR; Q42669; -.
DR   UniPathway; UPA00227; -.
DR   GO; GO:0005737; C:cytoplasm; 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:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
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.
FT   CHAIN           <1..764
FT                   /note="Aconitate hydratase"
FT                   /id="PRO_0000076653"
FT   BINDING         75..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         372
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         375
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         405
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         410
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         568
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         648..649
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   764 AA;  83274 MW;  E4A9B011FC6922F0 CRC64;
     HEAKTENAVQ ANMELEFKRN RERFGFLKWG SSAFHNMLVV PPGSGIVHQV NLEYLGRVVF
     NTNGLLYPDS VVGTDSHTTM IDGLGVAGWG VGGIEAEAAM LGQPMSMVLP GVVGFKLVGK
     LRNGVTATDL VLTVTQMLRK HGVVGKFVEF YGEGMGELSL ADRATIANMS PEYGATMGFF
     PVDHVTLQYL KLTGRKDETI SMIESYLLAN KMFVDYSEPQ VERVYSSHIE LNLSDVEPCI
     SGPKRPHDRV PLKEMKADWH ACLDNRVGFK GFAIPKEAQV KVAEFNFHGS PAQLRHGDVV
     IAAITSCTNT SSSVMLGAAL VAKKACELGL EVKPWIKTVL LQALGVVTKY LAKSGLQKYL
     NQLGFNIVGY GCTTCIGNSG DIDESVASAI TGNDIVAAAV LSGNRNFEGR VHPLTRANYL
     ASPPLVVAYA LAGTVDIDFE SEPIGVGKDG KKVFFRDIWP TSEEVAVVVN SNVLPDMFRA
     TYQAITEGNA TWNLLSVPEG TLYSWDPTST YIHEPPYFKD MSMSPPGPHG VKNAYCLLNF
     GDSITTDHIS PAGSIHKDSP AAKYLLERGV DRRDFNSYGV AVVMMRLWHV HFANIRIVNK
     LLKGEVGPKT IHIPSREKLS VFDAAMRYKS EGQDTIILAG AEYGIGSSRD WAAKGPMLLG
     VKAVIAKSFE RIHRSNLVGM GIIPLCFKAG EDADSLGLTG HERFTIDLPS NVGEIRPGQD
     VAVVTDTGKS FSCILRFDTE VELAYFDHGG ILQYVIRNLI HSKH