ID A0A0R3SH65_HYMDI Unreviewed; 843 AA.
AC A0A0R3SH65;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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};
GN ORFNames=HDID_LOCUS4275 {ECO:0000313|EMBL:VDL46684.1};
OS Hymenolepis diminuta (Rat tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000427901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HDID_0000427901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL46684.1, ECO:0000313|Proteomes:UP000274504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UYSG01001573; VDL46684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3SH65; -.
DR STRING; 6216.A0A0R3SH65; -.
DR WBParaSite; HDID_0000427901-mRNA-1; HDID_0000427901-mRNA-1; HDID_0000427901.
DR Proteomes; UP000046397; Unplaced.
DR Proteomes; UP000274504; 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; 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; 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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000274504};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 630..840
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 843 AA; 95496 MW; CAE12B443968CF31 CRC64;
MFPTRIAHLL RKSNLVHRSV LTSSRYQHKS AAEPFLNGSS SNYVEDIYAA WLKDPNSVHK
SWDVYFRGVL SGASLGFAYS SPPTLGFEHM SYMPVASPST RTSTSIGIGA KSIQDHLTVQ
TVIRSYQIRG HLAARLDPLD IKTSIESARD IVYGRYLGEA VLPEMDQVFH LPLTTHIGGD
QTELPFKEII KRLEDAYCQS IGVDYMFIND LEKCDWLRRR FETPGVTKLP NEERKLLLYR
LTQACKFEEY LAKKWSSEKR FGIEGCEVLI PAMKTVIDES VERGVDSFVV GMAHRGRLNV
LANVCHKPLS EIFCQFDPNL KAADEGSGDV KYHLGMSQHR VNRKTGKEFN IAVVANPSHL
EAVDPVVQGK TRAEQFYRKD FEGKHVMPIL LHGDASFAGQ GIVYETIHLA NLPSYTTHGT
VHIVVNNQIG FTTDPRMSRS SKHCTDVARV TSSPIFHVNA DDPEAVVHVA RVAAEWRATF
GTDVVIDLVG YRRFGHNETD EPMFTQPLMY KRIRQMPTVL EKYSKQLLSE RIITEQEFKD
AIEAYQTTCD GAYTEARAQT VTYNRSWIDS PWEKFFENRD PMNLPSTGIE ESQLNFIGEV
VSGYPQDFVV HPGLKRVLKG RADLVKNRLA DWALGEFFAY GSLLMSGHHV RVSGQDVERG
TFSHRHAVLH HQDIDQKMYV PLDNLSKDQA PFIICNSSLS EFAVMGFEMG YSLTNPNSLV
IWEAQFGDFA NGAQSIIDLY ICSGQQKWVR QSNLVLLLPH GMEGMGPEHS SGRMERLLQL
SNDDECYIPV VINENFSQQQ LLESNWILAN CTTPANMFHI LRRQILLPFR RPVRMRIPNV
ILN
//
