ID   A0A0N4Z6F6_PARTI        Unreviewed;      1020 AA.
AC   A0A0N4Z6F6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
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   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000276200.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0000276200.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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; A0A0N4Z6F6; -.
DR   STRING; 131310.A0A0N4Z6F6; -.
DR   WBParaSite; PTRK_0000276200.1; PTRK_0000276200.1; PTRK_0000276200.
DR   Proteomes; UP000038045; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          646..862
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          95..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1020 AA;  114886 MW;  A3A55BA22FCFBDDB CRC64;
     MLGGRFLVLN RKMHTMLKHA GRSINNPSIK NILQGVSPKF NGSRYLATSS NESFLSGASA
     NYVESMYEAW RENPDSVHKS WDIYFRNVEN GLTPGQAYTP PPTLAPGSSA VYSPSSAPAT
     SGRLDAKGVQ DHLNVQLLIR SYQTRGHNIA DLDPLGINSA DLDDTIPPEL ELSFYGFTEA
     DLDRQFILPP STYIGGTEKS LSLREIVKRL KSIYCQSTGI EYMHLNSYEQ QEWIRKQFET
     PAVSQLDQQA KRTLFKRLIR STKFEEFLAK KWPSEKRFGL EGCEVLIPAI KQVIDTSSAG
     GVESVVIGMP HRGRLNVLAN VCRQPLASIL SQFSTLEPSD EGSGDVKYHL GVCITRTNRQ
     TDKKIKVSVV ANPSHLEAVD PVVQGKVRAE AFYSGDSKCD HNLAIMLHGD AAFSGQGVVM
     ETFNLDDLPS YTIHGAIHIV CNNQIGFTTD PRSSRSSPYC TDVGRIVGCP IFHVNADDPE
     AVMHVCKVAA EWRRLFKKDV IIDLVSYRRH GHNELDEPMF TQPLMYQRIK QTKTVLDKYH
     KQIVADGAAD DNFVKEELTK YGNILETAYE EAQKITHVRH RDWLDSPWDD FFKGKNANSI
     PSTGVDKEAI DKVMSKFCSV PEGFNLHRGL DRTLKGRLQM LQENKVDWSI GEALAFGTLL
     KEGTHVRLSG QDVERGTFSH RHHVLHDQKI DQKVYNPLNN ISSDQAIYSV CNSSLSEYAV
     LGFEHGYSMV NPNSLVIWEA QFGDFSNTAQ CIIDQFISSG QSKWIRQSGL VMLLPHGYEG
     MGPEHSSARP ERYLQMCSED DQLNREAYPF NDEFEAKQLY ATNWIVANCT TPANFFHLLR
     RQVYMPFRKP LVVMTPKSLL RHPLARSPVD DFLPGTTFKR VIEEDGVASQ NPSAVQRLIF
     CTGKVYYDLI AARKHLGLED KVAVTRVEQM APYPYDLIDA ETKKYPNAEY VFAQEEHKNM
     GSWGFFQPRF LSLDKKCIYA GRKPSSSPAT GNKYTHLQEQ KHMLASVFNV DDKDLNGFKA
//