ID A0A061DF56_THECC Unreviewed; 900 AA.
AC A0A061DF56;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Aconitate hydratase {ECO:0000256|RuleBase:RU361275};
DE Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE EC=4.2.1.3 {ECO:0000256|RuleBase:RU361275};
GN ORFNames=TCM_000133 {ECO:0000313|EMBL:EOX90754.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX90754.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOX90754.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|RuleBase:RU361275}.
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:0000256|RuleBase:RU361275};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001879; EOX90754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061DF56; -.
DR STRING; 3641.A0A061DF56; -.
DR EnsemblPlants; EOX90754; EOX90754; TCM_000133.
DR Gramene; EOX90754; EOX90754; TCM_000133.
DR eggNOG; KOG0452; Eukaryota.
DR HOGENOM; CLU_013476_2_1_1; -.
DR InParanoid; A0A061DF56; -.
DR OMA; CLATTHD; -.
DR Proteomes; UP000026915; Chromosome 1.
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: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:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR CDD; cd01586; AcnA_IRP; 1.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 6.10.190.10; -; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
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 NCBIfam; TIGR01341; aconitase_1; 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR PANTHER; PTHR11670:SF62; ACONITATE HYDRATASE 1; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|RuleBase:RU361275};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275};
KW Lyase {ECO:0000256|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915}.
FT DOMAIN 65..568
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 697..825
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 900 AA; 98207 MW; AD751ECAEE79354A CRC64;
MATENPFNSI LKTLEKPGGG EFGKYYSLPA LDDPRIDKLP YSIKILLESA IRNCDEFQVK
SKDVEKIIDW ENTSPKQVEI PFKPARVLLQ DFTGVPAVVD LACMRDAMNN LGGNSNKINP
LVPVDLVIDH SVQVDVARSE NAVQANMELE FKRNKERFAF LKWGSNAFDN MLVVPPGSGI
VHQVNLEYLG RVVFNTNGVL YPDSVVGTDS HTTMIDGLGV AGWGVGGIEA EAAMLGQPMS
MVLPGVVGFK LLGKLRNGVT ATDLVLTVTQ MLRKHGVVGK FVEFYGEGMR ELSLADRATI
ANMSPEYGAT MGFFPVDHVT LQYLRLTGRS DETIAMIESY LRANKMFVDY SEPQTEKVYS
TYLDLKLEDV EPCISGPKRP HDRVPLKEMK ADWHACLDNR VGFKGFAIPK ESQNKVAKFS
FRGTPAELRH GDVVIAAITS CTNTSNPSVM LGAALVAKKA CELGLEVKPW IKTSLAPGSG
VVTKYLQKSG LQKYLNQLGF HIVGYGCTTC IGNSGDIDES VASAISENDM VAAAVLSGNR
NFEGRVHPLT RANYLASPPL VVAYALAGTV DIDFVTEPIG TAKDGKEIFF KDIWPSSEEV
ATVVHSSVLP DMFKATYEAI TKGNPMWNQL SVPSSTLYSW DPTSTYIHEP PYFKGMTMSP
PGPHGVKDAY CLLNLGDSIT TDHISPAGSI HKDSPAAKYL MEHGVDRRDF NSYGSRRGND
EIMARGTFAN IRIVNKLLKG EVGPKTIHIP TGEKLSVYDV AMRYKAAGQD TIILAGVEYG
SGSSRDWAAK GPVLLGVKAV IAKSFERIHR SNLVGMGIIP LCFKAGEDAD TLGLTGHERY
TIDLPNTVSE IRPGQDVTVA TDCGKSFTCT VRFDTEVELA YFNHGGILQY VIRNLIGSKQ
//
