ID A0A433TBW0_ELYCH Unreviewed; 1053 AA.
AC A0A433TBW0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=EGW08_013257 {ECO:0000313|EMBL:RUS79000.1};
OS Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC Plakobranchidae; Elysia.
OX NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS79000.1, ECO:0000313|Proteomes:UP000271974};
RN [1] {ECO:0000313|EMBL:RUS79000.1, ECO:0000313|Proteomes:UP000271974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC2010 {ECO:0000313|EMBL:RUS79000.1};
RC TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS79000.1};
RA Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL Submitted (JAN-2019) 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 -!- 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:RUS79000.1}.
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DR EMBL; RQTK01000478; RUS79000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433TBW0; -.
DR STRING; 188477.A0A433TBW0; -.
DR Proteomes; UP000271974; 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; 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; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 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:UP000271974};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 682..894
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1053 AA; 118486 MW; 3CA5D52A377ECC77 CRC64;
MLRIRDLLLR CPRGLSFANE QISATYAAHC SRSYASNGGS HSHSTGAVGR RQYATLSAAE
SFMNGSSSAY IEDMFEAWQK DPNSVHKSWD AFFRETGKGA PPGRAYVAPP TLRPSSGVPA
AYPAHAVEQG APVDEKTIED HLSVQSIIRA YQVRGHNISQ LDPLGICSAD LTSDTPPELF
TSTYKLSMGA RPCSHFQFVA SCLTHQDLDR VFRLPNTTYI GGGESVLPLR EIIRRLQHVY
CRSIGVEFMF INNLQQADWI RRKFETPGIM QFGPEERRML MARLIRSTRF EEFLARKWSS
EKRFGLEGCE VLIPAMKTII DSSSATGVDS FIIGMPHRGR LNVLANVCRK PLEKIICQFD
SKLEAADEGS GDVKYHLGMS HERVNRVTNK YIKIAVVANP SHLEAVDTVV QGKARAEMFY
RGDTDGKKVM PMLIHGDAAF SGQGIVYECL HLSDLPAFTT HGTVHIVVNN QIGFTTDPRS
SRSSPYCTDV ARVVNAPIFH VNADDPEAVI YVCKVASEWR ETFGKDVVID LASSFSTFKI
VCYRRFGHNE IDEPMFTQPL MYKKIAKQPT VLAKYAESLI NDAVVTQQEY EEEIAKYDKI
CEESYSLAKK ETAVSNIDWL DSPWSGFFEG RNPMEMPATG VHEETLQHIG KMFSTPPEDF
VIHGGLKRVL KARAKMVEER QADWALGEAF AFGSLLKEGI HVRLSGQDVE RGTFRCLHLL
LSTYSVGSLV WVQVVQRHHR LLVDVLVMQD VVPVAAQRER GFSITNPNAL VIWEAQFGDF
ANTAQCIIDQ FISSGQAKWV RQSGLVMLLP HGFEGMGPEH SSARLERFLQ MSNDDPDYFP
VEGPNFEMQQ LHDTNWFVCN FTTPANFFHA MRRQIALSFR KPLIVMTPKS LLRLPEARSS
FDDMVEGSRF QRLIPSTCEE PLNVKKIVFC SGRVYYELVK ERSQKQLNGE IALTRIEQLT
PFPFDLVKAE IQRFPNARLC WAQEEHKNAG AWSYVEPRLR TVCRKLGKPK KIEYAGRFSS
AAAATGNKQM HLMELSQLHN AAMDISPRPE GAY
//
