ID   ACOHC_CUCMA             Reviewed;         898 AA.
AC   P49608;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Aconitate hydratase, cytoplasmic;
DE            Short=Aconitase;
DE            EC=4.2.1.3;
DE   AltName: Full=Citrate hydro-lyase;
OS   Cucurbita maxima (Pumpkin) (Winter squash).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX   NCBI_TaxID=3661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Kurokawa Amakuri Nankin;
RX   PubMed=7640891;
RA   Hayashi M., de Bellis L., Alpi A., Nishimura M.;
RT   "Cytosolic aconitase participates in the glyoxylate cycle in etiolated
RT   pumpkin cotyledons.";
RL   Plant Cell Physiol. 36:669-680(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; D29629; BAA06108.1; -; mRNA.
DR   AlphaFoldDB; P49608; -.
DR   SMR; P49608; -.
DR   PRIDE; P49608; -.
DR   UniPathway; UPA00227; -.
DR   Proteomes; UP000504608; Unplaced.
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; Reference proteome.
FT   CHAIN           1..898
FT                   /note="Aconitate hydratase, cytoplasmic"
FT                   /id="PRO_0000076652"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         209..211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         441
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         507
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         510
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         540
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         545
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         703
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         784..785
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   898 AA;  98005 MW;  ADFE73173CA54971 CRC64;
     MAAENPFKEN LTSLPKPGGG EFGKYYSLPS LNDPRIDRLP YSIRILLESA IRNCDNFQVK
     KEDVEKIIDW ENSSPKQVEI PFKPARVLLQ DFTGVPAVVD LACMRDAMNK LGSDSNKINP
     LVPVDLVIDH SVQVDVARSE NAVQANMELE FQRNKERFAF LKWGSNAFQN MLVVPPGSGI
     VHQVNLEYLG RVVFNTSGLL YPDSVVGTDS HTTMIDGLGV AGWGVGGIEA EAAMLGQPMS
     MVLPGVVGFK LSGKLRNGVT ATDLVLTVTQ MLRKHGVVGK FVEFYGDGME ELSLADRATI
     ANMSPEYGAT MGFFPVDHVT LQYLKLTGRS DETVSMIEAY LRANKMFVDY KEPQQEKVYS
     SYLQLDLTDV EPCISGPKRP HDRVPLKEMK SDWHACLDNK VGFKGFAIPK EAQENVAKFS
     FHGQPAELKH GSVVIAAITS CTNTSNPSVM LGAALVAKKA CELGLQVKPW VKTSLAPGSG
     VVTKYLLKSG LQPYLNQQGF HIVGYGCTTC IGNSGDLDES VSAAISDNDI VAAAVLSGNR
     NFEGRVHPLT RANYLASPPL VVAYALAGTV DIDFEKEPIG KGKDGKDVYF RDIWPSTEEI
     AEVVQSSVLP DMFKSTYESI TKGNPMWNQL SVPSGTLYSW DPNSTYIHEP PYFKNMTMDP
     PGAHGVKDAY CLLNFGDSIT TDHISPAGSI HKDSPAAKYL LERGVDRKDF NSYGSRRGND
     EVMARGTFAN IRLVNKLLDG EVGPKTVHVP TGEKLSVFEA AEKYKSAGQD TIVLAGAEYG
     SGSSRDWAAK GPMLLGVKAV IAKSFERIHR SNLVGMGIIP LCFKSGEDAD SLGLTGHERY
     TIDLPDDISK IRPGQDVTVT TDSGKSFTCT VRFDTEVELA YFNNGGILPY VIRNLIKQ