IDH3A_DROME
ID IDH3A_DROME Reviewed; 377 AA.
AC Q9VWH4; E4NKP2; Q8IQW9; Q8SXH8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Probable isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial;
DE EC=1.1.1.41;
DE AltName: Full=Isocitric dehydrogenase subunit alpha;
DE AltName: Full=NAD(+)-specific ICDH subunit alpha;
DE Flags: Precursor;
GN Name=Idh3a {ECO:0000312|FlyBase:FBgn0027291};
GN Synonyms=l(1)G0156 {ECO:0000312|FlyBase:FBgn0027291};
GN ORFNames=CG12233 {ECO:0000312|FlyBase:FBgn0027291};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAN09496.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Hoskins R.,
RA Svirskas R., Rubin G., Celniker S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P56471};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterooligomer of subunits alpha, beta, and gamma in the
CC apparent ratio of 2:1:1. {ECO:0000250|UniProtKB:P56471}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=D;
CC IsoId=Q9VWH4-1; Sequence=Displayed;
CC Name=A {ECO:0000303|PubMed:10731132}; Synonyms=C;
CC IsoId=Q9VWH4-2; Sequence=VSP_050698;
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL90367.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF48965.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09496.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95545.1; -; Genomic_DNA.
DR EMBL; AY089629; AAL90367.1; ALT_FRAME; mRNA.
DR EMBL; BT125839; ADR83724.2; -; mRNA.
DR RefSeq; NP_001259705.1; NM_001272776.1. [Q9VWH4-1]
DR RefSeq; NP_573388.1; NM_133160.2. [Q9VWH4-2]
DR RefSeq; NP_728257.2; NM_167657.3. [Q9VWH4-2]
DR AlphaFoldDB; Q9VWH4; -.
DR SMR; Q9VWH4; -.
DR BioGRID; 59242; 82.
DR IntAct; Q9VWH4; 6.
DR STRING; 7227.FBpp0300338; -.
DR PRIDE; Q9VWH4; -.
DR DNASU; 32940; -.
DR EnsemblMetazoa; FBtr0074780; FBpp0074549; FBgn0027291. [Q9VWH4-2]
DR EnsemblMetazoa; FBtr0307904; FBpp0300338; FBgn0027291. [Q9VWH4-2]
DR EnsemblMetazoa; FBtr0336668; FBpp0307649; FBgn0027291. [Q9VWH4-1]
DR GeneID; 32940; -.
DR KEGG; dme:Dmel_CG12233; -.
DR CTD; 3419; -.
DR FlyBase; FBgn0027291; Idh3a.
DR VEuPathDB; VectorBase:FBgn0027291; -.
DR eggNOG; KOG0785; Eukaryota.
DR GeneTree; ENSGT00950000182989; -.
DR HOGENOM; CLU_031953_0_1_1; -.
DR InParanoid; Q9VWH4; -.
DR OMA; CVRPCRY; -.
DR PhylomeDB; Q9VWH4; -.
DR Reactome; R-DME-71403; Citric acid cycle (TCA cycle).
DR SignaLink; Q9VWH4; -.
DR BioGRID-ORCS; 32940; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32940; -.
DR PRO; PR:Q9VWH4; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0027291; Expressed in second segment of antenna (Drosophila) and 47 other tissues.
DR Genevisible; Q9VWH4; DM.
DR GO; GO:0005962; C:mitochondrial isocitrate dehydrogenase complex (NAD+); IEA:UniProt.
DR GO; GO:0005739; C:mitochondrion; HDA:FlyBase.
DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006102; P:isocitrate metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004434; Isocitrate_DH_NAD.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00175; mito_nad_idh; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW NAD; Oxidoreductase; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN ?..377
FT /note="Probable isocitrate dehydrogenase [NAD] subunit
FT alpha, mitochondrial"
FT /id="PRO_0000014442"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P50213"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P50213"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P50213"
FT SITE 169
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 216
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..32
FT /note="MAARFIQKILNQLGLIAARDAPAVTATPAVSQ -> MAARFIQKI (in
FT isoform A)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_050698"
SQ SEQUENCE 377 AA; 40844 MW; FB3F30905B8939B3 CRC64;
MAARFIQKIL NQLGLIAARD APAVTATPAV SQVNATPAAS RSYSSGTKKV TLIPGDGIGP
EISAAVQKIF TAANVPIEWE AVDVTPVRGP DGKFGIPQAA IDSVNTNKIG LKGPLMTPVG
KGHRSLNLAL RKEFNLYANV RPCRSLEGYK TLYDDVDVVT IRENTEGEYS GIEHEIVDGV
VQSIKLITEE ASKRVAEYAF QYAKNNNRKK VTVVHKANIM RMSDGLFLRC VRDMAQKFPE
IQFEEKYLDT VCLNMVQNPG KYDVLVMPNL YGDILSDMCA GLVGGLGLTP SGNMGLNGAL
FESVHGTAPD IAGKDLANPT ALLLSAVMML RHMELNTYAD KIERAAFETI KEGKYLTGDL
GGRAKCSEFT NEICAKL
