ID A0A081CI46_PSEA2 Unreviewed; 1039 AA.
AC A0A081CI46;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=PAN0_012d4564 {ECO:0000313|EMBL:GAK66342.1}, PSANT_06151
GN {ECO:0000313|EMBL:SPO48460.1};
OS Pseudozyma antarctica (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=84753 {ECO:0000313|EMBL:GAK66342.1, ECO:0000313|Proteomes:UP000053758};
RN [1] {ECO:0000313|Proteomes:UP000053758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10317 {ECO:0000313|Proteomes:UP000053758};
RA Saika A., Koike H., Hori T., Fukuoka T., Sato S., Habe H., Kitamoto D.,
RA Morita T.;
RT "Draft Genome Sequence of the Yeast Pseudozyma antarctica Type Strain
RT JCM10317, a Producer of the Glycolipid Biosurfactants, Mannosylerythritol
RT Lipids.";
RL Genome Announc. 2:e00878-e00814(2014).
RN [2] {ECO:0000313|EMBL:GAK66342.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 10317 {ECO:0000313|EMBL:GAK66342.1};
RA Morita T., Saika A., Koike H.;
RT "Draft genome sequence of the yeast Pseudozyma antarctica JCM 10317 known
RT as a producer of lipase B which used in a wide range of industrial
RT applications.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SPO48460.1, ECO:0000313|Proteomes:UP000325008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34888 {ECO:0000313|Proteomes:UP000325008}, and ATCC34888
RC {ECO:0000313|EMBL:SPO48460.1};
RA Guldener U.;
RL Submitted (MAR-2018) 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}.
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DR EMBL; DF830079; GAK66342.1; -; Genomic_DNA.
DR EMBL; OOIQ01000019; SPO48460.1; -; Genomic_DNA.
DR RefSeq; XP_014655587.1; XM_014800101.1.
DR AlphaFoldDB; A0A081CI46; -.
DR GeneID; 26305408; -.
DR HOGENOM; CLU_004709_1_0_1; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000053758; Unassembled WGS sequence.
DR Proteomes; UP000325008; 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:UP000053758};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 660..870
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 38..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1039 AA; 116901 MW; 39945FF892A1E46E CRC64;
MLRSITSRSM PRAAWRASTL PSASARIAKP TAFTASLRHY QSSSKSEQAS PAPAKPSAPT
GSDTFINTTN AYYAEEMHKL WKQDRSSVHA SWDVYFSGLA KGLPSEQAYR APPTLMPLPM
EAPPVDVSGF SGSTQAVDDH LKLQLLVRAY QVRGHRIARL DPLGILDPDL DPNVPEELKI
EHYGWSESDL DRKMRLGPGL LPNFVDSGIQ ELTIREIIDA CKRMYCGSIG VQYVHIPDRE
KCDWLRKRIE TPEPFKYSVE EKRTILDRLI WSDSFERFIA SKYPNEKRFG LEGGESLIPG
VKTLIDRSVE HGVESVTIGM PHRGRLNILA NVIRRPIEGI LHQFAGKEDD GEGGGDVKYH
LGANYVRPTP SGKKVALSLV ANPSHLEAED PVVLGKTRAL QDFAKDSEHK TSMALLMHGD
AAFAGQGVVY ETMGMYNLPY YATGGTVHIV VNNQIGFTTD PRFARSTPYP SDIAKSIDAP
IFHVNGDDVE AVTFVSQLAA DWRATFKKDV VIDLVCYRRH GHNETDQPSF TQPRMYAAIA
KQDPTLTKYA ARLVEEGSFT KSDIEEHQKW VWGMLEEAFD KSKNYQTEER EWLSSAWEGF
PSPKELREQI LDHKDTGVKE ETLKHIGKTV STYPEDFTVH RNLGRILKTR LKTVDEGKNI
DMSTGEALAF GSLALEGNYV RLSGQDVERG TFSQRHSVLH DQENEGTYTP LQHVGEGQAP
FVVCNSSLSE FGCMGFELGF SLVSPQNLTI WEAQFGDFAN NAQCIIDQFI ASGERKWLQR
TGLVLNLPHG YDGQGPEHSS ARIERFLQLC DDHPFRFPTP EKSNRQHQDS NMAVVYCTTP
ANYFHVLRRQ VHREFRKPLV NFFSKSLLRH PEARSNLEDF LPGTGFQRFI PEPHANEGKD
ELVAPDQIKR HILTFGQTYF ALLNHRRENN IKDVAISRIE QLSPLHYEAI VQALDKYPNA
DLVFCQEEPL NNGAWSYVQP RLRTACRHTQ HHKNDIVILA SRPPSSSVAT GSKVAHKAEV
EAYLRDAFDL NRKASDEGL
//
