ID F7VZI3_SORMK Unreviewed; 1019 AA.
AC F7VZI3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=SMAC_04160 {ECO:0000313|EMBL:CCC10931.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC10931.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC10931.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC10931.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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:CCC10931.1}.
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DR EMBL; CABT02000015; CCC10931.1; -; Genomic_DNA.
DR RefSeq; XP_003346728.1; XM_003346680.1.
DR AlphaFoldDB; F7VZI3; -.
DR STRING; 771870.F7VZI3; -.
DR GeneID; 10804115; -.
DR KEGG; smp:SMAC_04160; -.
DR VEuPathDB; FungiDB:SMAC_04160; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; F7VZI3; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000001881; 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:UP000001881};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 641..848
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 34..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1019 AA; 115141 MW; 5335D139A43E1657 CRC64;
MLRGSIRALQ TAGASKRCFS QVSQTTRATL KPAVGRRPMA VSQQRRNESA LHSPPDPNDN
FLSGSAANYI DEMYMQWKED PKSVHVSWQV YFKNMENGNM PISQAFQPPP TLVPGAANVV
PNIAAGAGVG IGEGANVTNH LKVQLLVRAY QARGHHKAKI DPLGIRNTDA SKGFGNIKPK
ELTPEYYGFT EKDLDTEYSL GPGILPRFAR DGREKMTLRE IVDACENIYC GSYGVEFIHI
PDREKCDWLR ERLEIPQPFK YSIDEKRRIL DRLIWSSSFE SFLATKYPND KRFGLEGCET
LVPGMKALID RSVDYGVKDI VIGMPHRGRL NVLSNVVRKP NEAIFSDDEE GSGDVKYHLG
MNFERPTPSG KRVQLSLVAN PSHLEAEDPV VLGKVRAIQH YNNDEKDHKS AMGVLLHGDA
AVAGQGIVYE CLGFHSLPAF STGGTIHLVV NNQIGFTTDP RFARSTAYCT DIAKAIDAPV
FHVNADDVEA VNFVCQLAAD WRAEFKQDVI IDLPLMYKRI NAKNPQIDTY VDQLLKEGTF
TKEDIEEHKQ WVWGMLEESF SKSKDYQPTS KEWTTSAWNG FKSPKELATE VLPHNPTAVN
KQTLEHIGTV IGSTPEGFQP HRNLKRILTN RTKSVVEGKG IDWATAEALA FGSLVNEGHH
VRISGQDVER GTFSQRHAVF HDQETEDTYT PLQHISKDQG KFVISNSSLS EYGILGFEYG
YSLQDPNGFN MWEAQFGDFA NTAQVIIDQF LASGESKWMQ RTGLVMSLPH GYDGQGPEHS
SARIERFLQL CNEDPRIYPS PEKLERQHQD CNMQVAYMTS PANLFHILRR QMKRQFRKRN
PRHLLLQVPP PPPRRSFRHR EFTDDAHFRW ILEDSAHKTG EIKAPEEIER VILCTGQVYA
ALLKHRQDNK IDNVAFTRIE QLHPFPWEQL RENLDQYPNA KTIVWAQEEP LNAGPWSYTQ
PRLETLLNHT KNHDRKHVMY AGRAPSASVA TGKKSSHLKE EKALVEMAFS VTQSKLKGE
//
