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Database: UniProt
Entry: A0A2T6ZCH2_TUBBO
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Original site: A0A2T6ZCH2_TUBBO 
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
//
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