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Database: UniProt
Entry: A0A0R3WKU6_HYDTA
LinkDB: A0A0R3WKU6_HYDTA
Original site: A0A0R3WKU6_HYDTA 
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
//
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