ID A0A158RE61_HYDTA Unreviewed; 785 AA.
AC A0A158RE61;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=TTAC_LOCUS6673 {ECO:0000313|EMBL:VDM30917.1};
OS Hydatigena taeniaeformis (Feline tapeworm) (Taenia taeniaeformis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Hydatigera.
OX NCBI_TaxID=6205 {ECO:0000313|Proteomes:UP000046396, ECO:0000313|WBParaSite:TTAC_0000668801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TTAC_0000668801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM30917.1, ECO:0000313|Proteomes:UP000274429}
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}.
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; UYWX01020314; VDM30917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158RE61; -.
DR STRING; 6205.A0A158RE61; -.
DR WBParaSite; TTAC_0000668801-mRNA-1; TTAC_0000668801-mRNA-1; TTAC_0000668801.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000046396; Unplaced.
DR Proteomes; UP000274429; 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:UP000274429};
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..712
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 785 AA; 85234 MW; F9BA26CB7653A3B4 CRC64;
MFSIDAALHA FPLHYFRYLR PSSIIRQIRS MSVCLSRFDC EILDYDKYCF ALKHVNETLA
RPLTFSEKVL YSHLSDPKAK DIVRGLSYLN LSPDRVAMQD ATAQMAILQF MSSGISRVAV
PTTIHCDHLV VARRGGDKDI SDAVASNKEI YDFLSSASAK FNIGFWLPGS GIIHQIMLEN
YCFPGALIIG TDSHTPNGGG LGGLCVGVGG SDAVDVMAGL DWELKCPKII GVELVGKLSG
WTSPKDVILK VADILTVKGG TGAIVEYFGP GVESISCTGM ATICNMGAEI GATTSVFPFN
DRMVDFLRAT GRGNIADLAS KYKSKLLSPD KGCVYDRVIK IDLNELEPHL NGPYTPDLAH
PISRLKSDAE AAGWPMEISV GLIGSCTNSS YEDMARAASV ARQALDHGIT NVATKFTVTP
GSEQIHATIE RDGLADTFRG IGGLVLANAC GPCIGQWDRK DKKHGEPNTI VTSYNRNFTG
RNDANPATHA FVASPEMVTA LVLGGNLGFN PLTDELMAPN GEKFKLKPPE GDTLPRNGFQ
RVDPHFQCPP SDGSGVQVTI SPTSDRLQVL SPFARWDGND LINMPILIKV RGKCTTDHIS
AAGAWLKFRG HLDNISNNMF IGAVNSENGE MNRVRHWPSG EWDTVPAVAR RYKAEGVPWV
VVGDANYGEG SSREHAALEP RHLGGRAIIV KSFARIHETN LKKQGMLPLT FVKSEDYDKI
QPSDKVSLLD LKSLAPGKTV RCRLTHADGS VEEIELAHTF NAKQLEWFIA GSALNRMKEV
ASCCS
//
