ID A0A0V0WZT1_9BILA Unreviewed; 1168 AA.
AC A0A0V0WZT1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=T06_13328 {ECO:0000313|EMBL:KRX81159.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX81159.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX81159.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX81159.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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 -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 2 family. {ECO:0000256|ARBA:ARBA00010800}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX81159.1}.
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DR EMBL; JYDK01000034; KRX81159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WZT1; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0030677; C:ribonuclease P complex; IEA:InterPro.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:InterPro.
DR GO; GO:0004526; F:ribonuclease P 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 GO; GO:0001682; P:tRNA 5'-leader removal; 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; 3.30.70.3250; Ribonuclease P, Pop5 subunit; 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; IPR002759; Pop5/Rpp14/Rnp2-like.
DR InterPro; IPR038085; Rnp2-like_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; PF01900; RNase_P_Rpp14; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF160350; Rnp2-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 649..863
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1168 AA; 132127 MW; D6D8E328F3047F47 CRC64;
MLSRTSRFKQ LLQLSQCIAS NVRRCQSTGY GAPPNFPAPM SRMAAEPFLN GTSSIYIEEM
FESWKNDPKS VHKSWDAFFR SVEAGMQPGD AYYPPPSLSA LSHHVASIDT NTISDHAKVQ
QLIKSYQTRG HHIADLDPLG INKADLDDTV APELELSTYN LTEKDLNREF LLPNTTYIGG
DRSVLTLGEI LQRLKKIYCH HIGVEYMHLS NREQYLWIRK HFETPSIMEL TPDEQKRLFK
RLIRSTKHVL FLNLNYQLIM VIKICRFEEF LAKKWPAEKR FGLEGCEVLI PAMKQVIDCT
AALGVDTFVI GMPHRGRLNI LANVCRQELE AIFCQFSTLQ PEDEGSGDVK YHLGVCIERL
NSASGKPIKI SVVANPSHLE AVDPVVQGKT RAEQFYRNDT RGDKVMSILL HGDAAFSGQG
IVYETFDISG LPAYTCHGSI HFIVNNQIGF TTDPRFSRSS PYCTDVAKVV NAPIFHVNAD
DPEAVMHVCT VASQWRNKFK KDVVIDLVCY RRHGHNEQDE PSFTQPLMYQ KIAKALPVMD
KYAQKLINAG VVNQEYVQAE MDHYVEIMET AYSNSQKEMF VRNRDWLDSP WKTFFPCDVD
LKLKPTGVSV EVLQHIGNIF SAVPKNFRLH SGLERVLRGR AQMVQSGTSD WALAEAFAFG
SLLGEGFHVR LSGQDVERGT FSHRHHVLHD QNVDKNTVEP LNELWPGKQA QYTVCNSSLS
EFGVLGFEVG FSLSNPNALV IWEAQFGDFS NNAQCIFDQF ISSGQAKWIR QSGIVCLLPH
GYEGMGPEHS SARLERFLQL CSDDEERMKP PGPEFEGGQL METNMIVANC TTPANFFHLL
RRQMLLPFRK PLIVMTPKSL LRHPEARSPF DDYLENTRFK RLIPEDGPAS ENPEQVKRLV
FCSGKLYYEL KKERDNKKLD SDVAICRIEQ LSPFPYDLVK EQAEKYKNAQ LIWAQEEHKN
MGAWLYVHPR LLTALNNGRS VKYAGRAPSA STATGNKYHH MREQNKVIAD TLEVTMPGVH
HYQMVKAKYR YCVFQVILDP SVELPHSSVT SSTIYGAVTA AIKSVFGECG LGQCKHLLKV
KVFEDELGIV VIRVLDAHLQ TLITSTPFIR QISRIPAILK CLFIGGSIRA CAKATLNYHR
NNLIKDLPKA SLSDSSIIMN TLKSFYMA
//
