ID A0A0N0BHZ2_9HYME Unreviewed; 1012 AA.
AC A0A0N0BHZ2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=WN51_10375 {ECO:0000313|EMBL:KOX76981.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX76981.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX76981.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX76981.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX76981.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ435736; KOX76981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0BHZ2; -.
DR STRING; 166423.A0A0N0BHZ2; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000053105; 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 Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 648..862
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 40..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1012 AA; 114281 MW; 748753FCFF9C45C9 CRC64;
MTNSQYLDHM YQSWRKNPNS VSSSWDSYFR SIYADNLPES ATSTPPADSN QSVTSTSARN
STPSMTSTPK DSTPSTVSAS IRIESSSNII PSNLVGAQSS APSQQNVRSQ SNGGIQGESF
INGALDINAT IRAYQTRGHL IADTDPLRIQ NPESYKLQGT SNLPPAIVVR QHLKGMTEAD
MDREFPLAPF TVIGGPKRSL PLREILTRLN QIYCGHLGLE YIYIHDLVVL DWLRDKFEVP
GAWELPADHK KFIWMNIMRA VTFEGFLARK FPTEKRFGLE GCESFIPSLI QCLETSAEHG
VESAVIGMAH RGRLNTLSNV CFKPLHQLLT QFNPIPLEGF GSGDVKYHLG THAERTLERS
KKKILIAMMA NPSHLEAING VVIGRVRAGQ VEENDAQYGK KSMAILVHGD AAFSGQGVVY
ETMHLTNLPN YTTGGVIHLV INNQVKRSEM HVMVLKQGPE ETLLRHQKLK KQSLKKLQPH
SRESALRTQR KSRRATFHND VVLDIVGYRR FGHNELDEPM LTQPLMYKRI KEHPNVLSIY
SDKLLKDGVI TEAFAKEEIE KYWNYCEMEF EKAKTIDSMQ LSDWHDVPWS KFFSDQSPKN
KIPPTGIDIE TIKTICKAIS TPPHGITPHA QVLRVMEKRN QLMEARQADW AIGEALAFLS
LLKEGHHVRL SGQDVERGTF SHRMHIIHDQ HRDKTFKNIL HNVFPGQGLY TVSNSSLSEY
GVCTFEIGYS AYNHNTLTMW EAQFGDFCNT CQVAIDTILS SGQTKWGRQV GLVLLLPHGL
EGQGPEHSSA RLERFLELCD DDCVHMPGET VEEIMTRQLF EINWIICNLT TSANLFHCLR
RQIHMPFRKP LCIMTPKSLL RHPMAISPFS DMESGTSFKP LLSDPYVKLG NIQKVLMCSG
KVYYDLITER EGKQLEDKIA VIRIEQICPF PYHFLAQEMM KYPNAKIMWF QEEHKNQGAY
AYVRDRIALA LGKKLEEVTY GGRPPSASPA TGSKVIHSTE YKDIMAAAMK LD
//
