ID A0A195E7Y8_9HYME Unreviewed; 1102 AA.
AC A0A195E7Y8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=ALC57_06854 {ECO:0000313|EMBL:KYN20947.1};
OS Trachymyrmex cornetzi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN20947.1, ECO:0000313|Proteomes:UP000078492};
RN [1] {ECO:0000313|EMBL:KYN20947.1, ECO:0000313|Proteomes:UP000078492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN20947.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN20947.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex cornetzi WGS genome.";
RL Submitted (SEP-2015) 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; KQ979568; KYN20947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195E7Y8; -.
DR STRING; 471704.A0A195E7Y8; -.
DR Proteomes; UP000078492; 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; 2.
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; 2.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 3.
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 Reference proteome {ECO:0000313|Proteomes:UP000078492};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 692..905
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1046..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1102 AA; 123785 MW; CD77A57989752626 CRC64;
MYKARTVFST LAPLAPRICG PERYASWVVR SHPLTRTSQL ILTEPARKYN SRVATEPFLN
GSTSSYVEEM YNAWLQDPNS VHVSWDSFFR NSTAGAAPGF AYQAPPSLAP SYNQVPLGAL
LPLGGATQLG QAPVNEKIID DHLAVQAIIR SYQARGHLVA DLDPLGIMQT DLIHTHYAAR
KGSPEQIRGH HIAKLDPLGI NSADLDDRHP QELLYTHYSF EESDMDRVFK LPSTTFIGGK
EKSLSLREIL KRLEAAYCGH IGVEFMFINS LEQCNWIRQK METPGIMEMT NDEKRLILAR
LTRATGFEAF LARKWSSEKR FGLEGCEILI PAMKQVIDKS TELGVESIVM GMPHRGRLNV
LANVCRKPLS QIFTQFAALE AADDGSGDVK YHLGTYIERL NRVTNKNIRL AVVANPSHLE
AVDPVVQGKT RAEQFYRGDG EGKKVMSILL HGDAAFCGQG IVFETMHLSD LPDYTTHGTV
HIVVNNQIGF TTDPRHSRSS PYCTDVARVV NAPIFHVNSD DPEAVMHVCK VAAEWRATFH
KDVVIDLVSY RRNGHNEIDE PMFTQPLMYR KIKNTLSALD KYANSLIDST VVTPAEVEDV
KAKYEKICEE AYNNARQETH IKYKDWLDSP WSGFFEGKDP LKVSPTGIKE DTLIHIGKKF
SSPPPNAAEF VIHKGIERIL KSRMEMIEAR TVDWALGEAM AFGSLLKEGI HVRLSGQDVE
RGTFSHRHHV LHHQTVDKAT YRPLCYLYPD QAPYTVCNSS LSEFGVLGFE LGYSMTNPNA
LVCWEAQFGD FNNTAQCIID QFISSGQAKW VRQSGLVMLQ PHGLEGMGPE HSSARLERFL
QMSADDPDYF PPESEEFAVR QLHDSNWIVA NCSTPANYFH ILRRQIALPF RKPLILMTPK
SLLRHPEAKS NFDLMLEDTQ FLRVIPEEGA AVQNPNGVKR LLFCSGKVYY DLKKARTERN
LEDKVAIARV EQISPFPYDL VKIEAAKYPN AELIWAQEEH KNQGAWTYVQ PRFHTALNGI
RNVVSASNSN GQGWFAGLFS STKPIETTTV SKPQATESTE PTEPKQRTVR YAGRPTASSP
ATGSKMQHLK ELKQLLDDSL NF
//
