ID F8Q1B4_SERL3 Unreviewed; 1000 AA.
AC F8Q1B4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=SERLA73DRAFT_123478 {ECO:0000313|EMBL:EGN98092.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
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; GL945481; EGN98092.1; -; Genomic_DNA.
DR AlphaFoldDB; F8Q1B4; -.
DR STRING; 936435.F8Q1B4; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; F8Q1B4; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000008063; 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:UP000008063};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 634..844
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1000 AA; 112321 MW; AAF16DEDE72019FB CRC64;
MIPRQALRHF PHARLAACGG RQLLVRALAT PASPPSPNDP FANGTNAYYA EEMYKHWRND
PKSVHASWDV YFSGLDQGLP SAKAFQPPPS LMAPPADGAP ALHAGGGAEL DDHLKVQLLV
RAYQVRGHHV AELDPLGILD ADLADVHPPE LELSRYGFTE RDLDKQIALG PGILPHFATE
DRKTMSLREI IKLLKRIYCG AVGIQYVHIP DKEQCDWIRE RVEIPKPWNY TLEEKRMILD
RLIWSESFEK FIASKYPNEK RFGLEGCEAL IPGMKALIDR SVDHGVKHVT IGMPHRGRLN
VLGNVIRKPT EAILNEFSGS QSDDSPAGDV KYHLGANYVR PTPSGKKVSL SLVANPSHLE
AGDPVVLGKT FAIQNLEQDE TTHNTAMGVL LHGDAAFAGQ GIVYETMGFH NLPNYGTGGT
IHLIVNNQIG FTTDPRFARS TPYPSDIAKS IDAPIFHVNG DNVEAVNFVC QLAADYRAKY
KRDVVVDIVC YRRYGHNETD QPSFTQPRMY QAIEKQPTPL TQYAKFLIGR GTFTEKDIEE
HKKWVWGMLE KAAGAAKDYV PTSKEWLSAS WQGFPSPRQL AEETLPTRAT GSDEETLKRI
GKAISQYPSG FTPHRNLARI LSTRGKTVEE GRNIDWSTAE ALAFGSLALE KIHVRVSGQD
VERGTFSQRH AVIHDQVNEQ QYIPLNDLGS NQARFVVCNS SLSEYGTLGF ELGYSLVSPS
SLTIWEAQFG DFANNAQCII DQFIAAGERK WLQRTGLVMS LPHGYDGQGP EHSSGRIERF
LQLCDDHPHL YPTPKKIERQ HQDCNMQVVY PTTPANYFHV LRRQIHRDFR KPLILFFSKS
LLRHPRARSD LTEMIGDTHF QRYIGDPHPN DLVQPENVRR HILCTGQVYH ALLQEREDKG
IKDVAISRIE QLSPFPYDLI TPHLDKYPNA DLLWCQEEPL NNGAWTYVGP RILTAANETQ
YHRGKYPYYA GREPTSSVAT GSKIQHKKEI EEFLAAAFAT
//
