ID G4TPS7_SERID Unreviewed; 998 AA.
AC G4TPS7;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=PIIN_07275 {ECO:0000313|EMBL:CCA73320.1};
OS Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS (Piriformospora indica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Sebacinales; Serendipitaceae; Serendipita.
OX NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA73320.1, ECO:0000313|Proteomes:UP000007148};
RN [1] {ECO:0000313|EMBL:CCA73320.1, ECO:0000313|Proteomes:UP000007148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA73320.1,
RC ECO:0000313|Proteomes:UP000007148};
RX PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA Kogel K.H.;
RT "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT the Mutualistic Root Symbiont Piriformospora indica.";
RL PLoS Pathog. 7:e1002290-e1002290(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}.
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:CCA73320.1}.
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DR EMBL; CAFZ01000216; CCA73320.1; -; Genomic_DNA.
DR AlphaFoldDB; G4TPS7; -.
DR STRING; 1109443.G4TPS7; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; G4TPS7; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000007148; 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:UP000007148};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 631..841
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 998 AA; 112731 MW; BBB928399E821F5B CRC64;
MLARRCTRQL SSALRCNPTA AFRTRLRCLA TAATTFENGT NNYYAQEMYR SWKQDPSSVH
ASWNAYFSAL DKGLGSDQAF QLPPSLHNVP QPAGGAPTLH MHGDKELTDA LKVQLLVRAY
QVRGHHVANL DPLGILDPDL SPARPIELEL SHYGFTEADL KKEFSLGPGI LPHFAKNGVS
SMTLEDIIKT CKRVYCRAIG YQYIHIPDKE QCDWIRERVE IPNPWSYSVE EKRMILDRLM
WSEMFEKFIA SKYPNEKRFG LEGCESLIPG MKALIDRSVE HGVKHVIMGM PHRGRLNVLA
NVIRKPIEAI LNEFSGGVHG EDAGGDVKYH LGANYVRPTP SGKRVSLSLV ANPSHLEAED
PLVLGKTRAI QHFENDEFNH NTALGVLLHG DAAFAGQGVV YETMGFHNLP SYGTGGTIHL
IVNNQIGFTT DPRFSRSTPY CSDIAKAIDA PIFHVNGDNV EAVTFVCQLA ADWRAKYKKD
VVVDIICYRR YGHNETDQPS FTQPRMYKAI EKQPTPLTQY TNFLSKQKTF TDQDIEEHRK
WVWGMLEKAA AGAKTYEPSP KEWLSSEWPN FPSPKELAEN NLPHLPTGVA EETLKHIGKV
ISSYPEGFNV HRNLARILQT RGKTVEEGTN IDMSTAEALA MGALVLEKID VRISGQDVER
GTFSQRHAVL HDQATERQYV PLKNLGKDQA AFTACNSSLS EYGVLGFELG YSLVSPASLV
IWEAQFGDFA NNAQVIIDQF IASGERKWLQ RTGLVMSMPH GYDGQGPEHS SGRIERFLQL
CDDHPHIFPP PEKLARQHQD CNMQIVYPTT PANYFHVLRR QIHREFRKPL ILFFSKSLLR
HPQARSDLSE MTGETHFQRY LPEPHPEQLV APEEIRRHIL CTGQVYYTLL KEREARQAWD
VAISRLEQLS PFPYDLLTPH LDKYPNADLM WCQEEPLNCG AWTYVGTRIL TAANETEHHK
GKYPYYAGRP PYSSVATGSK AQHMKEVSQL VEQAFAPR
//
