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
//