ID N1QE38_SPHMS Unreviewed; 1053 AA.
AC N1QE38;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=SEPMUDRAFT_127260 {ECO:0000313|EMBL:EMF10576.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF10576.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF10576.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF10576.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB456267; EMF10576.1; -; Genomic_DNA.
DR RefSeq; XP_016758697.1; XM_016902139.1.
DR AlphaFoldDB; N1QE38; -.
DR STRING; 692275.N1QE38; -.
DR GeneID; 27899276; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_0_1; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000016931; 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:UP000016931};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 673..883
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1053 AA; 118125 MW; 2137418EE0A519F0 CRC64;
MLLSQLSRCS KRLASGSSAR AFSSAAPQSA PRTALITKRR ELGVSSYNAF TAHHRQYAQA
AERTDQGVDP SDSFLTGNTA GYVDEMYSEW QRDPSSVHVS WQHYFKNMES GDMPVSRAFT
PPPTIVPPPA GGVIAPSGAV GAAAGQSSEV LNHLKVQLLV RAYQARGHHK AKIDPLGIKD
LNKSTPKELE LKTYNFTEKD MDMELTLGPG ILPRFAKDGR EKMTLREIID ACERLYCGPY
GVEYIHIADR EQCDWLRERV EVPQPYKYSV DEKRRILDRL IWSSSFESFL ATKYPNDKRF
GLEGGESLIP GMKALIDRSV DYGVKDIVIG MPHRGRLNVL SNVVRKPNES IFSEFGGSAE
PSDEGSGDVK YHLGMNFERP TPSGKRVQLS LVANPSHLEA EDPVVLGKTR AILHYNNDEE
KATSAMGVLL HGDAAFAAQG IVYETMGFVG LPAYQTGGTI HLIVNNQIGF TTDPRFARST
PYCSDLAKFV EAPIFHVNGD DVEALNFVCQ LAADWRAEFK KDVVVDIVCY RKQGHNETDQ
PSFTQPLMYK KINEQLPVLD KYTQQLLDAK TFTKEDIEEH KSWVWGMLEE SFAKSKDYQP
NSREWLTSAW NGFKSPKELA TEILPHEPTA VDADTLKQVA KVIGQPPEGF QVHKNLKRIL
ANRTKSVEEG KNIDMSTGEA LAFGTLVKEG HHVRVSGQDV ERGTFSQRHA VLHDQESEGT
YTPLKHISED QGSFVIANSS LSEYGALGFE YGYSLSSPTA LVIWEAQFGD FANNAQCVID
QFIASGEVKW LQRSGLVMNL PHGYDGQGPE HSSGRMERFL QLCNEDPRIF PAPEKLDRQH
QDCNMQIVYC TTPANSFHIL RRQMNRQFRK PLISFFSKSL LRHPLARSKI EDFTGDSAFQ
WIIPDPAHEA DAAFQIDSHD KIERVILCSG QVFAALFKHR ETNDIKNTAI VRLEQLNPFP
WAQLKENLDS YPNAQNIVWC QEEPLNAGAW SFTQPRIETL LNHTEHHDRK HVMYAGRNPS
ASVATGLKSS HLLEEKRLLE DAFSVKQDKL KGE
//
