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Database: UniProt
Entry: F7D575_XENTR
LinkDB: F7D575_XENTR
Original site: F7D575_XENTR 
ID   F7D575_XENTR            Unreviewed;       363 AA.
AC   F7D575;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 4.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Isocitrate dehydrogenase [NAD] subunit, mitochondrial {ECO:0000256|RuleBase:RU361266};
GN   Name=idh3g {ECO:0000313|Ensembl:ENSXETP00000001625};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000001625};
RN   [1] {ECO:0000313|Ensembl:ENSXETP00000001625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000001625};
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2] {ECO:0000313|Ensembl:ENSXETP00000001625}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUN-2011) to UniProtKB.
CC   -!- SUBUNIT: Heterooligomer of subunits alpha (IDH3A), beta (IDH3B), and
CC       gamma (IDH3G) in the apparent ratio of 2:1:1. The heterodimer
CC       containing one IDH3A and one IDH3B subunit and the heterodimer
CC       containing one IDH3A and one IDH3G subunit assemble into a
CC       heterotetramer (which contains two subunits of IDH3A, one of IDH3B and
CC       one of IDH3G) and further into the heterooctamer.
CC       {ECO:0000256|ARBA:ARBA00011525}.
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   AlphaFoldDB; F7D575; -.
DR   Ensembl; ENSXETT00000001625; ENSXETP00000001625; ENSXETG00000000731.
DR   AGR; Xenbase:XB-GENE-492840; -.
DR   Xenbase; XB-GENE-492840; idh3g.
DR   eggNOG; KOG0784; Eukaryota.
DR   HOGENOM; CLU_031953_0_0_1; -.
DR   TreeFam; TF315033; -.
DR   Bgee; ENSXETG00000000731; Expressed in skeletal muscle tissue and 14 other cell types or tissues.
DR   ExpressionAtlas; F7D575; differential.
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:SF42; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT GAMMA, 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   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          25..349
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   363 AA;  39912 MW;  4DB5519541BBADA6 CRC64;
     RELLCHLPSL KFIWPPPAKY GGRHTVTMIP GDGIGPELML HVKEVFRHSC VPIDFEVVNV
     NSTSNDEDDI QNAITAIRRN RVALKGNIET NHNMPPSHRS RNNLLRTSLD LYANVIHCRS
     VPGVQTRHKD IDIMIVRENT EGEYSSLEHE SVSGVVESLK IITRANSLRI AEYAFKLARE
     EGRKKITAVH KANIMKLGDG LFLACCKEVA SGYPDITFES MIVDNTTMQL VSNPQQFDVM
     VMPNLYGNIV NNVCAGLVGG PGLVPGANYG NVYAVFETAT RNTGKSIANK NIANPTAMLL
     ASCMMLDHLK LHSYAASIRK AILGSMNEHR MHTADIGGQG TTSEVVQSIC RQIIVKNGRA
     VTV
//
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