ID A0A0P9IQE0_RHOGW Unreviewed; 968 AA.
AC A0A0P9IQE0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-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=RHOBADRAFT_30823 {ECO:0000313|EMBL:KPV71647.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV71647.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV71647.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV71647.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
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; KQ474092; KPV71647.1; -; Genomic_DNA.
DR RefSeq; XP_018267696.1; XM_018412927.1.
DR AlphaFoldDB; A0A0P9IQE0; -.
DR STRING; 578459.A0A0P9IQE0; -.
DR GeneID; 28973376; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000053890; 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:UP000053890};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 584..794
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 968 AA; 108587 MW; 1DB0273C8D760964 CRC64;
MLEEWKQDPS SVHASWRAYF ELTEGGLPAS QAFQAPPIAI GDSMEGPAPV LLNMGGGGQI
EDHMKVQLLV RAFQVRGHHI AKLDPLGMSH ADLDGTTPSE LTLEHYGWTE KDLDKEFELG
AGILPRFKKA GTDKMTLRQI MDTCKKIYCG SIGIQYIHIP NRDECDWIRE RIEIPNPYNY
STEEKKAILD RLVWSDSFER FIASKYPNEK RFGLEGCESL VPGMKALIDR SVDHGVKSVV
MGMPHRGRLN VLANVVRKPT EAILAEFAPS QDPNEEAAAD VKYHLGANYV RPTPNGKRVA
LSLVANPSHL EAANGVVLGK TKALQHFEGE ADPSTAMGLL LHGDAAFAGQ GVVYETMGFA
DLPNYGTGGT VHIVVNNQIG FTTNPSQGRS TPYPSDIAKA IDAPIFHVNA DDVEAVTYVC
QLAADWRAKF RKDVVVDLVC YRRHGHNEGD QPMFTQPKMY ETIKNQPTTL SLYTKQLVEE
KSFTDEETEK HKSWVWGLLE ESFDKSKEYK PTSKEWLSSS WDGFPSPREL KENVLEARPT
GVDFDTLKHV GKTISSYPDG FNVHRNLQRI LKTRGTSIEE GKNIDYSTAE ALAFGTLALE
KVHVRVSGQD VERGTFSQRH AVLHDQKTDE QYVPLKHLGE GQGPVTVCNS SLSEYGVLGF
ELGYSLVDPA LLVIWEAQFG DFANGAQIMI DQFIAAGERK WLQRSGLTLS LPHGYDGQGP
EHSSARIERF LQLCDDHPFI YPTPEKQARQ VQDCNLQIVY PTIPSNIFHA LRRQIHRDYR
KPLVVTFSKN LLRHPQARSS LEEFGPDTHF QRYIAEAEPE GFAAPDDVVR HILCSGQVYY
TLLAEREKRG LKNVAISRVE QLSPLPYDLI TPHLDRYPNA TTYWVQEEPI NNGAWTYVQP
RIETAMRETQ HHKTRRVYFA GRGPTSSVAT GSKKQHALEI EQFCAAAFDL EAHRVEFDSQ
SAHKKGDF
//
