ID   A0A182FCB1_ANOAL        Unreviewed;      1200 AA.
AC   A0A182FCB1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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};
OS   Anopheles albimanus (New world malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7167 {ECO:0000313|EnsemblMetazoa:AALB004145-PA, ECO:0000313|Proteomes:UP000069272};
RN   [1] {ECO:0000313|EnsemblMetazoa:AALB004145-PA}
RP   IDENTIFICATION.
RC   STRAIN=STECLA/ALBI9_A {ECO:0000313|EnsemblMetazoa:AALB004145-PA};
RG   EnsemblMetazoa;
RL   Submitted (AUG-2022) to UniProtKB.
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   AlphaFoldDB; A0A182FCB1; -.
DR   STRING; 7167.A0A182FCB1; -.
DR   EnsemblMetazoa; AALB004145-RA; AALB004145-PA; AALB004145.
DR   VEuPathDB; VectorBase:AALB004145; -.
DR   VEuPathDB; VectorBase:AALB20_027427; -.
DR   Proteomes; UP000069272; Chromosome 3L.
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   1200 AA;  133207 MW;  8C0372868CBB8E15 CRC64;
     MHRARTALHL VNPMGQQNFG SFLLKKPASK LTTELVAASS VKLYNSTAAE PFLNGSSSNY
     IDDMYNAWLR DPASVHASWD AYFRNNSYSA PPSLAPVPKN HVPAAQYLGG SSLPAVAGAG
     AAIGGRIDDK LIDDHLAVQA IIRSYQIRGH NVARLDPLGI NSADLDDKTP PELLYSSYRF
     EEADMERVFK LPSTTFIGGK EKFLPLREIL GRLEKAYCNK IGVEFMFINS LEQCNWIRER
     FETPNIMNYS NDEKRLILAR LTRATGFEAF LAKKFSSEKR FGLEGCEIMI PAMKEVIDVS
     TRLGVESIIM GMPHRGRLNV LANVCRKPLH QIFTQFAGLE AADDGSGDVK YHLGTYIERL
     NRVTNKNIRL AVVANPSHLE AVDPVVQGKT RAEQFYRGDG EGKKVMSILL HGDAAFCGQG
     VVFETMHLSD LPDYTTHGTV HIVVNNQIGF TTDPRHSRSS PYCTDVARVV NAPIFHVNGD
     DPEAVMHVCK VAAEWRATFH KDVIIDIVSY RRNGHNEIDE PMFTQPLMYK KIRGTKPALD
     IYANQLIGEG VVTAEEVKSV KDKYEKICEE AFEQAKTETH IKYKDWIDSP WSGFFEGKDP
     LKVAPTGVIE ETLVHIGNRF SSPPPNAAEF VIHKGLLRVL AARKEMLENK TIDWALAEAM
     AFGSLLKEGI HVRLSGQDVE RGTFSHRHHV LHHQTVDKAT YRPLCHLYPD QAPYTVCNSS
     LSEFGVLGFE LGYSMTNPNA LVCWEAQFGD FNNTAQCIID QFVSSGQAKW VRQSGLVMLL
     PHGMEGMGPE HSSARVERFL QMCSDDPDYF PPESDEFAIR QLHDINWIVA NCSTPGNYFH
     LLRRQIALPF RKPLIVLTPK SLLRHPECRS NFSEMTEGTE FQRLIPDALT AENPNAVKRV
     IFCTGRVYYD LLKARRDRQL DSSIAISRIE QISPFPYDLV KAECAKYPNA ELVWAQEEHK
     NQGCWTYVQP RFDTAINSTR DFSVEDDGAN EGYKDVFEAY KPKNRPSTGN AAAATPQNAK
     DSSGYKACSS SAASAPESLS SPSDSAAEPG SSWFSRWFGS SSSSSSSSNS KSNAAASRQT
     ESTTEITPTT TSFPSSSNIT PTNDNRSQNA NVHNHNHHAR IDSVQEERLV QQKTGQGFNI
     PQGTFNSPTS GSAASKGRKV RISSRPLSYV GRPCGASTAT GSKAQHVKEL KNLLDDAMAL
//