ID A0A2T6ZCH2_TUBBO Unreviewed; 1066 AA.
AC A0A2T6ZCH2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
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=B9Z19DRAFT_1135702 {ECO:0000313|EMBL:PUU73190.1};
OS Tuber borchii (White truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=42251 {ECO:0000313|EMBL:PUU73190.1, ECO:0000313|Proteomes:UP000244722};
RN [1] {ECO:0000313|EMBL:PUU73190.1, ECO:0000313|Proteomes:UP000244722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tbo3840 {ECO:0000313|EMBL:PUU73190.1,
RC ECO:0000313|Proteomes:UP000244722};
RG DOE Joint Genome Institute;
RA Murat C., Kuo A., Barry K.W., Clum A., Dockter R.B., Fauchery L., Iotti M.,
RA Kohler A., Labutti K., Lindquist E.A., Lipzen A., Ohm R.A., Wang M.,
RA Grigoriev I.V., Zambonelli A., Martin F.M.;
RT "Draft genome sequence of Tuber borchii Vittad., a whitish edible
RT truffle.";
RL Submitted (APR-2017) 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:PUU73190.1}.
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DR EMBL; NESQ01000405; PUU73190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6ZCH2; -.
DR STRING; 42251.A0A2T6ZCH2; -.
DR Proteomes; UP000244722; 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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 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:UP000244722};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 695..905
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1066 AA; 119567 MW; 52846D8ABC44F7F5 CRC64;
MLRSALRSSC RHSGSSLALG SSRSLTTASL AKQLIPQATA TRRPTSLTAH KRCLNLVSRN
NSTDASSKGV DPSDSFLQGN TANYIDEMYL SWKRDPSSVH ISWQVYFRNM EGDGPASQAF
QAPPTLVPTP TGGVPSLVPG AHLGGNTDVT KHLKVQLLVR AYQVRGHHKA NIDPLGIRSG
ADLNGTSKPR ELDLDHYQFT EKDLDDEYTL GPGILPRFAV DGKEKMTLRE IISACEKTYC
GSYGIEYVHI ADRDQCDWIR ERVEIPTPWE YDNHEKRRIL DRLIWSSSFE SFLSNKYPND
KRFGLEGCEA LVPGMKALID RSVDRGVKDI IIGMPHRGRL NVLSNVVRKP NESIFSEFGG
TAEPSDEGSG DVKYHLGMNF ERPTPSGKRV QLSLVANPSH LEAEDPVVLG KTRAIQHFNN
DEKSHNSAMG VLVHGDAAFA AQGIVYETMG FHALPGYSTG GTIHLIVNNQ IGFTTDPRFA
RSTPYCSDIA KSIDAPIFHV NADDVEAVNF VCELASDWRA QFKRDVVIDM VCYRKYGHNE
TDQPSFTQPL MYRKIAEKQH ALDRYIAQLL KEGTFTENDI QEHKGWVWSM LEDSFAKSRE
YQPTAREWLT SAWNGSFANK ISKNDEQVLS RITGFKTPKE LSTEVLPHLP TAIEESQLKH
IGDVIGSVPE EFSVHRNLSR ILSNRKKVVD EGTGIDWSTA EALAFGSLLM EGQHVRVSGQ
DVERGTFSQR HAVLHDQENE NTYTPLQHLS DAQASFVISN SSLSEFGVLG FEYGYSLSSP
DALVIWEAQF GDFANNAQCI IDQFIASGES KWFQRTGIVM SLPHGYDGQG PEHSSGRMER
YLQLCNEDPR EFPCPTKLDR QHQDCNMQIA YMTSPSNLFH ILRRQMKRQF RKPLIIFFSK
SLLRHPIARS ELSEFTGDSH FRWFIPETDH GKGIKDPVEC KRLLFCTGQV YAALVKQRAA
SGVDDVAIAR IEQLHPFPWA QIRDELQKYP NLEEIIWTQE EPLNAGAWTF VQPRLETILR
QTENHSAKHV KYAGRAPSAS VATGMKSTHL KEEQALVNDA LGISPH
//