ID H2Q9W0_PANTR Unreviewed; 366 AA.
AC H2Q9W0; A0A2J8KCN4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit, mitochondrial {ECO:0000256|RuleBase:RU361266};
GN Name=IDH3A {ECO:0000313|EMBL:JAA10864.1,
GN ECO:0000313|Ensembl:ENSPTRP00000012542.4,
GN ECO:0000313|VGNC:VGNC:10253};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000012542.4, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000012542.4, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:JAA10864.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA10864.1}, and Smooth
RC vascular {ECO:0000313|EMBL:JAA19870.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000012542.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalytic subunit of the enzyme which catalyzes the
CC decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The
CC heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and
CC the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G)
CC subunits, have considerable basal activity but the full activity of the
CC heterotetramer (containing two subunits of IDH3A, one of IDH3B and one
CC of IDH3G) requires the assembly and cooperative function of both
CC heterodimers. {ECO:0000256|ARBA:ARBA00037577}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH;
CC Xref=Rhea:RHEA:23632, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.41;
CC Evidence={ECO:0000256|ARBA:ARBA00037023};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23633;
CC Evidence={ECO:0000256|ARBA:ARBA00037023};
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 -!- 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; AACZ04065419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABC01000474; JAA10864.1; -; mRNA.
DR EMBL; GABF01002275; JAA19870.1; -; mRNA.
DR RefSeq; XP_510524.3; XM_510524.6.
DR STRING; 9598.ENSPTRP00000068408; -.
DR PaxDb; 9598-ENSPTRP00000012542; -.
DR Ensembl; ENSPTRT00000013530.5; ENSPTRP00000012542.4; ENSPTRG00000007336.6.
DR GeneID; 453565; -.
DR CTD; 3419; -.
DR VGNC; VGNC:10253; IDH3A.
DR eggNOG; KOG0785; Eukaryota.
DR GeneTree; ENSGT00950000182989; -.
DR HOGENOM; CLU_031953_0_1_1; -.
DR OMA; CVRPCRY; -.
DR OrthoDB; 143577at2759; -.
DR TreeFam; TF105692; -.
DR Proteomes; UP000002277; Chromosome 15.
DR Bgee; ENSPTRG00000007336; Expressed in thymus and 21 other cell types or tissues.
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 2: Evidence at transcript level;
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:UP000002277};
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 33..358
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 366 AA; 39609 MW; 46B49E4AC6936D5F CRC64;
MAGSAWISKV SRLLGAFHNP KQVTRGFTGG VQTVTLIPGD GIGPEISAAV MKIFDAAKAP
IQWEERNVTA IQGPGGKWMI PSEAKESMDK NKMGLKGPLK TPIAAGHPSM NLLLRKTFDL
YANVRPCVSI EGYKTPYTDV NIVTIRENTE GEYSGIEHVI VDGVVQSIKL ITEGASKRIA
EFAFEYARNN HRSNVTAVHK ANIMRMSDGL FLQKCREVAE NCKDIKFNEM YLDTVCLNMV
QDPSQFDVLV MPNLYGDILS DLCAGLIGGL GVTPSGNIGA NGVAIFESVH GTAPDIAGKD
MANPTALLLS AVMMLRHMGL FDHAARIEAA CFATIKDGKS LTKDLGGNAK CSDFTEEICR
RVKDLD
//
