ID   Q175A3_AEDAE            Unreviewed;      1057 AA.
AC   Q175A3;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040267};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00042984};
GN   ORFNames=AAEL006721 {ECO:0000313|EMBL:EAT41628.1};
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT41628.1, ECO:0000313|Proteomes:UP000682892};
RN   [1] {ECO:0000313|EMBL:EAT41628.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:EAT41628.1};
RA   Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA   Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA   Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T.,
RA   Rogers Y.-H., Kravitz S., Fraser C.M.;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAT41628.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Liverpool {ECO:0000313|EMBL:EAT41628.1};
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA   Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA   Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA   Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA   Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA   El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA   Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA   Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA   Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA   Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA   Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA   Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA   Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(2007).
RN   [3] {ECO:0000313|EMBL:EAT41628.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:EAT41628.1};
RG   VectorBase;
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC       overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC       contains multiple copies of three enzymatic components: 2-oxoglutarate
CC       dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC       lipoamide dehydrogenase (E3). {ECO:0000256|ARBA:ARBA00037426}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006936}.
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DR   EMBL; CH477404; EAT41628.1; -; Genomic_DNA.
DR   RefSeq; XP_001652169.1; XM_001652119.1.
DR   AlphaFoldDB; Q175A3; -.
DR   STRING; 7159.Q175A3; -.
DR   PaxDb; 7159-AAEL006721-PA; -.
DR   VEuPathDB; VectorBase:AAEL006721; -.
DR   eggNOG; KOG0450; Eukaryota.
DR   OMA; RDSYCRT; -.
DR   PhylomeDB; Q175A3; -.
DR   Proteomes; UP000682892; Unassembled WGS sequence.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 2.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          652..865
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1057 AA;  118618 MW;  E13E21D38EF8F7AB CRC64;
     MHRARTALQL IGHPAGQQSF GSWLIRNPSS KLTGELVAAS SVKLYNSAAA EPFLNGSSSN
     YIDDMYNAWL RDPASVHASW DAYFRNNSYE APPSLAPIPR NHVPASQYLG SAVPALAGGS
     SAVGTRIDDK LIDDHLAVQA IIRSYQIRGH NISKLDPLGI SNVDLDDRIP TELLYSSYRF
     EEADMDRVFK LPSTTFIGGK EKFLPLREIL SRLERAYCNK IGVEFMFINS LEQCNWIRER
     FETPNIMNYT NEEKRLLLAR LTRATGFEAF LAKKFSSEKR FGLEGCEIMI PAMKEVIDVS
     TRLGVESIIM GMPHRGRLNV LANVCRKPLN QIFTQFAGLE AADDGSGDVK YHLGTYIERL
     NRVTNKNIRL AVVANPSHLE AVDPVVQGKT RAEQFYRGDG EGKKVMSILL HGDAAFSGQG
     VVYETMHLSD LPDYTTHGTV HIVVNNQIGF TTDPRHSRSS PYCTDVARVV NAPIFHVNSD
     DPEAVMHVCR VAAEWRATFH KDVIIDLVSY RRNGHNEIDE PMFTQPLMYK KIRGIKPVLD
     IYANQLIAEG CVTADEVKSV KDKYEKICDE AMEQAKVETH IKYKDWLDSP WSGFFEGKDP
     LKVAPTGVIE ETLVHIGNRF SCPPPNAAEF AIHKGLMRVL AARKEMVDNK TVDWALGEAM
     AFGSLLKEGI HVRLSGQDVE RGTFSHRHHV LHHQTVDKAT YRPLCHLYPD QAPYTVCNSS
     LSEFGVLGFE LGYSMTNPNA LVIWEAQFGD FNNTAQCIID QFISSGQSKW VRQSGLVMLL
     PHGMEGMGPE HSSARAERFL QMCSDDPDYF PPESEEFAIR QLHDINWIVA NCSTPANYFH
     IMRRQIALPF RKPLVLLTPK SLLRHPEARS SFSEMTDGTE FQRIIPDASA ASENPTSVKK
     LIFCSGRVYY DLTKARKERK LDSDIAISRL EQISPFPYDL IKAECAKYPN AELVWAQEEH
     KNQGYWTYIE PRFDTAINST RDLSVQDKLV LQKTAHGFNI SEGTFNTPTD GTRGRKVKIS
     SRPLSYVGRP CSASTATGSK AQHTKELKNL LDNAMAL
//