ID A0A0L7RJ31_9HYME Unreviewed; 1112 AA.
AC A0A0L7RJ31;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=WH47_06796 {ECO:0000313|EMBL:KOC70756.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC70756.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC70756.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC70756.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-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; KQ414583; KOC70756.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7RJ31; -.
DR STRING; 597456.A0A0L7RJ31; -.
DR Proteomes; UP000053825; 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:UP000053825};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 704..917
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1112 AA; 125245 MW; CB5481E781BAD78A CRC64;
MLTEPIRKYN SRVATEPFLN GSSSSYVEEM YNAWLQDPHS VHVSWDSFFR SSTAGAAPGL
AYQAPPSLAP SHNQVPLGAL LPLGGGSQLS QIPVNEKIID DHLAVQAIIR SYQARGHLVA
DLDPLGIMQS DLVHTHYAAR KGSPEQVLRQ YMLGKASSQT DSLNNYFSSH VYYKVKIRGH
HIAKLDPLGI NSADLDDRHP QELLYNHYAF GNREHTTTYS QELQYRVAAL TKKESDMDRI
FKLPSTTFIG GKEKSLPLRE ILKRLENAYC GHIGVEFMFI NSLEQCNWIR QKMETPGIME
VTNDERRLIL ARLTRATGFE AFLARKWSSE KRFGLEGCEI LIPAMKQVID KSTELGVESV
VMGMPHRGRL NVLANVCRKP LSQIFTQFAA LEAADDGSGD VKYHLGTYIE RLNRVTNKNI
RLAVVANPSH LEAVDSVVQG KTRAEQFYRG DGEGKKVMSI LLHGDAAFCG QGIVFETMHL
SDLPDYTTHG TIHIVVNNQI GFTTDPRHSR SSPYCTDVAR VVNAPIFHVN SDDPVAVMHV
CKVAAEWRAT FHKDVVIDIV SYRRNGHNEI DEPMFTQPLM YRKIKNTPPV LDKYAKSLID
DCVVTAEEVK DVKDKYEKIC EEAYTNARQE THIKYKDWLD SPWSGFFEGK DPLKVSPTGI
KEDTLIHIGK KFSSPPPNAA EFVVHKGIER ILKSRMEMIE ARTVDWALGE AMAFGSLLKE
GIHVRLSGQD VERGTFSHRH HVLHHQTVDK ATYRPLCYLY PDQAPYTVCN SSLSEFGVLG
FELGYSMTNP NALVCWEAQF GDFNNTAQCI IDQFISSGQA KWVRQSGLVM LQPHGLEGMG
PEHSSARLER FLQMSADDPD YFPPESEEFA VRQLHDINWI VANCSTPANY FHILRRQIAL
PFRKPLILMT PKSLLRHPEA KSSFDLMLEN TEFLRVIPEE GVASQNPSNV KRVLFCSGKV
YYELKKARAE KKLDDKVAIA RVEQISPFPY DLVKKEAAKY PNAELAWAQE EHKNQGAWTY
VQPRFHTALN GTRTVSSGNS SYKGEGSGGW FSNWFSSTKP TTVSEPLPVE SDKPKQRTLR
YVGRPTAASP ATGSKMQHLK ELKQLLDESF DV
//
