ID A0A1Q5SXX5_9EURO Unreviewed; 1060 AA.
AC A0A1Q5SXX5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=PENSUB_12787 {ECO:0000313|EMBL:OKO92802.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKO92802.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKO92802.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKO92802.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) 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:OKO92802.1}.
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DR EMBL; MNBE01000740; OKO92802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5SXX5; -.
DR STRING; 1316194.A0A1Q5SXX5; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000186955; 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:UP000186955};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 683..893
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1060 AA; 119326 MW; 109AC6E92EC28D68 CRC64;
MFRNTALKAT HSNMLRGVAS STSRRAFHLT STARSASKTS TFGLTSRRPL AVVDRAFNGA
RLYASSAEGN APGVDPNDSF LQGSTANYID EMYLAWKRDP SSVHISWQTY FKNMEDGNMP
ISQAFTPPPT LVPTPTGGVP QDMPGHGLSA GADVTNHLKV QLLCRAYQAR GHHKAKIDPL
GIRGDAEAFG YSKPKELELD HYGFTERDLD QEFALGPGIL PRFLTETRKK MTLREIIAAC
EKIYCGSYGV EYIHIPDRKP CEWIRDRFEI PEPYNYSVDD KRRILDRLIW SSSFESFLAT
KFPNDKRFGL EGCETLVPGM KALIDRSVDY GIKDIVIGMP HRGRLNVLSN VVRKPNESIF
SEFAGSTEPS DEGSGDVKYH LGMNFERPTP SGKRVQLSLV ANPSHLEAED PVVLGKTRAI
QHYNNDETKF DSAMGVLLHG DAAFAAQGVV YETMGFHSLP AYSTGGTIHI VVNNQIGFTT
DPRFARSTPY CSDIAKSIDA PVFHVNADDV EAVNYVCQVA ADWRAEFKSD VVVDIVCYRK
QGHNETDQPS FTQPLMYKRI ASQKAQLDKY IEKLINEGTF TKEDIDEHKK WVWGMLNDSF
DRSKDYQPTG KEWLTSAWNN FKTPKELATE VLPHLETAVE TKSLQHIADK VSGSSVPEGF
TLHRNLKRIL ANRKKSVDEG KNIDWATAEA LAFGSLVDEG YHVRISGQDV ERGTFSQRHA
VLHDQETEAT YTPLQNITDK QGSFVISNSS LSEFGTLGFE YGYSLTSPEA LVMWEAQFGD
FANNAQCIID QFIAAGESKW LQRSGLVVSL PHGYDGQGPE HSSGRMERWL QLCNEEPRVF
PSADKLDRQH QDCNMQIVYM TEPSNIFHVL RRQMHRQFRK PLVIFFSKAL LRHPIARSDL
EAFTGDSHFQ WIIRDPAHKT EAIEAPEKIE RVIMCSGQVY AALVKHREAN GIRNTAITRV
EQLHPFPWDQ LKENLDSYPN AKDIVWCQEE PLNAGAWSYV QPRIETMLNS TEHHNRRHVL
YAGRAPSASV ATGLKAVHLK EEQEFLEDAF SVHQDRLKGE
//
