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Database: UniProt
Entry: A0A0G2IC88_9PEZI
LinkDB: A0A0G2IC88_9PEZI
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ID   A0A0G2IC88_9PEZI        Unreviewed;      1036 AA.
AC   A0A0G2IC88;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-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=UCDDA912_g02650 {ECO:0000313|EMBL:KKY37305.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY37305.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY37305.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY37305.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY37305.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY37305.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) 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:KKY37305.1}.
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DR   EMBL; LCUC01000090; KKY37305.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2IC88; -.
DR   STRING; 1214573.A0A0G2IC88; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000034680; 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:UP000034680};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          659..869
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1036 AA;  116993 MW;  1ACEC0C7271B3D9E CRC64;
     MQRLCRASSA ALRATRSQCL SKPSSSLCAA RRPLALSTQK RYKSALFNAP DPNDNFLQGE
     NANYIDEMYV QYKQDPKSVH VSWQVYFKNI ESGNMPISQA FQPPPNLVPS SSAAVTGLAA
     GAGVGIGEGS DIDNHLKVQL LVRAYQARGH HKARIDPLGI RQEQKGFGNI KPKELELDYY
     QFTEKDLDTE YTLGPGILPR FKRDGREKMT LREIIDACER IYCGSFGAEF IHIPDREKCD
     WLRERIEVPK PFTYSHDEKR RILDRLIWSS SFESFLATKY PNDKRFGLEG CETLVPGMKA
     LIDRSVDYGV KDIIIGMPHR GRLNVLSNVV RKPNESIFSE FAGTSAAEDE GSGDVKYHLG
     MNFERPTPSG KRVQLSLVAN PSHLEAEDPV VLGKARAIQH YNNDEKTHRT AMGVLLHGDA
     AFAAQGVVYE CLGFQSLPAY STGGTIHIVV NNQIGFTTDP RFARSTAYCT DIAKAIDAPV
     FHVNADDVEA VNFVSQLAAD WRAEFQSDVV IDLVCYRKHG HNETDQPSFT QPLMYKRIQS
     HDPQIDIYVD KLLQDGTFTK EDIEEHKKWV WGMLEESFSK SKDYQPTSKE WTTSAWNGFK
     SPKELASEVL PHLPTAVRKD TLDHIGEMIG GAPEGFNIHR NLKRILSNRT KTVLEGKNID
     WSTAEALAFG SLVSEGHHVR VAGQDVERGT FSQRHAVFHD QESEDTYTPL QHISKDQGKF
     VISNSSLSEY GAMGFEYGYS LSSPNALVMW EAQFGDFANN AQCVIDQFIA SGEVKWMQRT
     GLVLSLPHGY DGQGPEHSSG RIERYLQLCN EDPRIFPSED KLQRQHQDCN MQIAYMTTPA
     NLFHVLRRQM NRQFRKPLII FFSKSLLRHP LARSNIEDFT GDSQFQWIIE DPAHETGELK
     PREEIDRVVI CSGQVYTALH KYRADNGIKD VAITRIEQLN PFPWQQLKEN LDSYPNAKTI
     VWAQEEPLNA GAWSFTQPRI ETLLNETQHH DHKHVMYAGR NPSASVATGL KANHVKEEQE
     LLEVAFTVTQ DKLKGE
//
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