ID A0A0R3WKU6_HYDTA Unreviewed; 361 AA.
AC A0A0R3WKU6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit, mitochondrial {ECO:0000256|RuleBase:RU361266};
GN ORFNames=TTAC_LOCUS1348 {ECO:0000313|EMBL:VDM17852.1};
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_0000136101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TTAC_0000136101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM17852.1, 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU361266}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769,
CC ECO:0000256|RuleBase:RU361266}.
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DR EMBL; UYWX01000271; VDM17852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3WKU6; -.
DR STRING; 6205.A0A0R3WKU6; -.
DR WBParaSite; TTAC_0000136101-mRNA-1; TTAC_0000136101-mRNA-1; TTAC_0000136101.
DR Proteomes; UP000046396; Unplaced.
DR Proteomes; UP000274429; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004434; Isocitrate_DH_NAD.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR NCBIfam; TIGR00175; mito_nad_idh; 1.
DR PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR PANTHER; PTHR11835:SF34; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|RuleBase:RU361266};
KW Reference proteome {ECO:0000313|Proteomes:UP000274429};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW ECO:0000256|RuleBase:RU361266};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU361266}.
FT DOMAIN 28..352
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 361 AA; 39046 MW; 46794E5593DDD9A5 CRC64;
MSLSKGLRRL SSARVHILRC RFYSGIRTVA LIPGDGIGPE ISSAVKKIFA VANVPIKFAT
VDVTPTRLPD GTFGMPPESL DVIRKLGIGL KGPLATPIGK GHGSLNLALR KEFNLYANVR
PCKSVEGYET PYKGVDLVTI RENTEGEYSG IEHVIVDGVV QSIKVITYEA SSRVAEFAFK
FAQDNGRSTV TAVHKANVMR MSDGMFLRAC REQAERYPNI HFREMFLDSV CLGMVQDPLQ
FDVLVMPNLY GDILSDLAAG LVGGLGVTPS GNIGQQGALF ESVHGTAPNI AGQDKANPTA
LLFSATMMLR HLDLSHYANL IEASVFSVLH AKKHLTMDLG GTAKCSEYTA AICEEIVRGP
H
//