ID A0A074ZZ26_9TREM Unreviewed; 397 AA.
AC A0A074ZZ26;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit, mitochondrial {ECO:0000256|RuleBase:RU361266};
GN ORFNames=T265_02546 {ECO:0000313|EMBL:KER31232.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER31232.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER31232.1, ECO:0000313|Proteomes:UP000054324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT "Opisthorchis viverrini - life in the bile duct.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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; KL596649; KER31232.1; -; Genomic_DNA.
DR RefSeq; XP_009165073.1; XM_009166809.1.
DR AlphaFoldDB; A0A074ZZ26; -.
DR STRING; 6198.A0A074ZZ26; -.
DR GeneID; 20316734; -.
DR KEGG; ovi:T265_02546; -.
DR CTD; 20316734; -.
DR OrthoDB; 143577at2759; -.
DR Proteomes; UP000054324; 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:SF80; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT BETA, 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 Mitochondrion {ECO:0000256|RuleBase:RU361266};
KW Reference proteome {ECO:0000313|Proteomes:UP000054324};
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 48..372
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 397 AA; 43530 MW; 58CEA77B615F79A7 CRC64;
MFGVHACVPE GAAGGDRPSP PITDDDVVYL ASALNACSYA TATLRKKTVT LIPGDGVWPE
LFLSVRNVFQ EFGIPVEFEE VRLNGLSSVA SDDLNFAIQS LNKTKVGLKG IIRTPVGRRE
VKTVNMILRR MLDLYANVVH VRSVPGIPNR HGPLDFAIIR EQLEGEYSCL EHESVPGVVE
CLKIMTRYNC ERIAKFAFDY AVRNNRTTVT AVHKANIMKL GDGLFLDTCQ QVSKLYPHIT
FKSMIIDNCC MQLASRPKQF DVLVMPNLYG NIVDNLAAGL VGGAGVVPGV SYSHEIAVFE
PGTRHSYAEA SGRDIANPTA ILLASCDLLR HVNLNEHAAK LESAIYKVVE SGQVLTTDVG
GRSTTSDFIE ALLRQYRADA RSNRDPTTSI PRLPRKS
//
