ID A0A0V0YES9_TRIPS Unreviewed; 786 AA.
AC A0A0V0YES9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 Name=Rad50 {ECO:0000313|EMBL:KRX98870.1};
GN ORFNames=T4E_2803 {ECO:0000313|EMBL:KRX98870.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX98870.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX98870.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX98870.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX98870.1}.
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DR EMBL; JYDU01000018; KRX98865.1; -; Genomic_DNA.
DR EMBL; JYDU01000018; KRX98866.1; -; Genomic_DNA.
DR EMBL; JYDU01000018; KRX98868.1; -; Genomic_DNA.
DR EMBL; JYDU01000018; KRX98869.1; -; Genomic_DNA.
DR EMBL; JYDU01000018; KRX98870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0YES9; -.
DR STRING; 6337.A0A0V0YES9; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000054815; 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 CDD; cd01584; AcnA_Mitochondrial; 1.
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:UP000054815};
KW Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 73..509
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 590..717
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 786 AA; 86536 MW; 55F0B7068DADCA61 CRC64;
MNISVINLFF NGTKIMGFRQ FNSARFLHKS STHFATQVPI SRFELDKFLP YDDLIQRLDI
VRKRLNRPLT LAEKILYSHL DDPENAEIVR GSSYLKLRPD RVAMQDATAQ MAVLQFISSG
LNSVSVPTTI HCDHLIEANE EANSDLKRAK DVNAEVYEFL SSVAAKYGIG FWHPGSGIIH
QIILENYAFP GLLLIGTDSH TPNGGGLCGL CIGVGGADAV DVMADIPWEL KCPKVMGVKL
QGQLSGWTSP KDVILKLAEI LTVKGGTGYI IEYFGPGVDS ISCTGMGTIC NMGAEVGATT
SVFPFTNRMK RYLEATGREG IATAAEKCKH LFTSDAGAGY DQLVEINLSE LEPRINGPFT
PDLGHTIHNL GQHARENGYP LEVKAGLIGS CTNSSYEDMT RAANVAQQAV EHNYKAKSIF
DVTPGSEQIR ATMERDGLTE TFRKIGATVL ANACGPCIGQ WNRKDVRKGE KNTIVTSYNR
NFTGRNDANP ATHAFVASPE IVTAIALAGR LDFDPTRDYL TANDGRKFKL KVPVGEELPS
KGFDRGQETY QAPPADGSAV KVVVQPNSKR LQLLKAFDKW DGKDFEDMFV LIKIKGKCTT
DHISAAGPWL KFRGHLDNIS NNMFIGAINE ENGEMNKVKN QLSGEWSSVP EAARFYKAKG
KKWIVFGEEN YGEGSSREHA ALEPRHLGGR AIVVKSFARI HETNLKKQGM LALTFVNPAD
YHKVLPTDSV SLVGLKDFKP GKPLKCILKH HDGSTDEFLL DHTYNDLQIE WFKAGSALNY
MAAKRK
//
