ID A0A0R3VW15_TAEAS Unreviewed; 786 AA.
AC A0A0R3VW15;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Aconitate hydratase, mitochondrial {ECO:0000256|RuleBase:RU362107};
DE Short=Aconitase {ECO:0000256|RuleBase:RU362107};
DE EC=4.2.1.3 {ECO:0000256|RuleBase:RU362107};
GN ORFNames=TASK_LOCUS1609 {ECO:0000313|EMBL:VDK23339.1};
OS Taenia asiatica (Asian tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000160801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TASK_0000160801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK23339.1, ECO:0000313|Proteomes:UP000282613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|ARBA:ARBA00003113}.
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:RU362107};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU362107};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000256|RuleBase:RU362107};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU362107}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU362107}.
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DR EMBL; UYRS01000472; VDK23339.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3VW15; -.
DR STRING; 60517.A0A0R3VW15; -.
DR WBParaSite; TASK_0000160801-mRNA-1; TASK_0000160801-mRNA-1; TASK_0000160801.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000046400; Unplaced.
DR Proteomes; UP000282613; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 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 NCBIfam; TIGR01340; aconitase_mito; 1.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 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 Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362107};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU362107};
KW Lyase {ECO:0000256|RuleBase:RU362107};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362107};
KW Mitochondrion {ECO:0000256|RuleBase:RU362107};
KW Reference proteome {ECO:0000313|Proteomes:UP000282613};
KW Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 67..504
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 584..713
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 786 AA; 84756 MW; F9634FB0CFF68B38 CRC64;
MLPGRAASCS LSLQCFRHLK PSLAIGQKRC LSVLLSRFDS KILDYEKYCF ALRSVNETLA
RPLTLSEKIL YSHLSDPKTK DIARGSSYLN LSPDRVTMQD ATAQMAILQF MSSGLSRVAV
PTTVHCDHLV VAHKGSDKDL SNAVTSNKEV YDFLSSASAK FNIGFWHPGS GIIHQIMLEN
YCFPGALIIG TDSHTPNGGG LGGLCVGVGG ADAVDVMAGL DWELKCPKVI GVELVGKLSG
WTSPKDVILK VADILTVKGG TGAIIEYFGP GVESISCTGM ATICNMGAEI GATTSVFPFN
DRMVDFLRAT GRKDIADLAS KYKSKLLSPD KGCIYDRVIK IDLGELEPHL NGPYTPDLAH
PISKLKSDAE AAGWPMEISA GLIGSCTNSS YEDMARAASV ARQALEHGIT NVATKLIVTP
GSEQIHATIE RDGLADAFRG IGGLVLANAC GPCIGQWDRK DKKRGEPNTI VTSYNRNFTG
RNDANPATHA FVASPEVVTA LVLGGNLGFN PLTDELTAAN GTKFKLKPPE GDTLPRNGFQ
RVDPHFQCPP ADGSHVQVTI SPTSDRLQAL SPFARWDGND LIDMPILIKV RGKCTTDHIS
AAGPWLKFRG HLDNISNNMF IGAVNSENGE VNRVCHRPSG EWDTVPAVAR RYKAEGVPWV
VIGEVNYGEG SSREHAALEP RHLGGRAIIV KSFARIHETN LKKQGMLPLT FVNPDDYDKV
QPSDKVSLLG LKSLALGKTV RCRLTHADGS SEEIELTHTF NANQLGWFVA GSALNHMKET
TSCHHQ
//
