ID M3YCH4_MUSPF Unreviewed; 383 AA.
AC M3YCH4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit, mitochondrial {ECO:0000256|RuleBase:RU361266};
GN Name=IDH3B {ECO:0000313|RefSeq:XP_004772974.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000009031.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000009031.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004772974.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004772974.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Plays a structural role to facilitate the assembly and ensure
CC the full activity of the enzyme catalyzing the decarboxylation of
CC isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of
CC the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer
CC composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have
CC considerable basal activity but the full activity of the heterotetramer
CC (containing two subunits of IDH3A, one of IDH3B and one of IDH3G)
CC requires the assembly and cooperative function of both heterodimers.
CC {ECO:0000256|ARBA:ARBA00037063}.
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 EMBL; AEYP01079656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004772974.1; XM_004772917.3.
DR STRING; 9669.ENSMPUP00000009031; -.
DR Ensembl; ENSMPUT00000009182.1; ENSMPUP00000009031.1; ENSMPUG00000009107.1.
DR GeneID; 101675188; -.
DR CTD; 3420; -.
DR eggNOG; KOG0784; Eukaryota.
DR GeneTree; ENSGT00950000182989; -.
DR HOGENOM; CLU_031953_0_1_1; -.
DR OMA; TCAHKAN; -.
DR OrthoDB; 143577at2759; -.
DR Proteomes; UP000000715; Unplaced.
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:UP000000715};
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 50..376
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 383 AA; 42017 MW; 18F9A373F66E2B32 CRC64;
MAARIGVRCL TRALVAAPNP GAWRSLCTSA VAQAASRSQA EDMRVEGAFP VTMLPGDGVG
PELMHAVKEV FKAASVPVEF QEHHLSEVQN MASEEKLEQV LSSMKENKVA IIGKIHTPME
YKGELASYDM RLRRKLDLFA NVVHVKSLPG YKTRHNNLDL VIIREQTEGE YSSLEHESAR
GVIECLKIVT RTKSQRIAKF AFDYATKKGR GKVTAVHKAN IMKLGDGLFL QCCEEVAELY
PKIKFETMII DNCCMQLVQN PYQFDVLVMP NLYGNIIDNL AAGLVGGAGV VPGESYSAEY
AVFETGARHP FAQAVGRNIA NPTAMLLSAS NMLRHLNLEY HSNMIADAVK KVIKVGKVRT
SDMGGYATCQ DFTEAVIGAL PQP
//
