ID G8Y521_PICSO Unreviewed; 998 AA.
AC G8Y521;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 Name=Piso0_005419 {ECO:0000313|EMBL:CCE85789.1};
GN ORFNames=GNLVRS01_PISO0M14312g {ECO:0000313|EMBL:CCE85789.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE85789.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
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}.
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DR EMBL; FO082047; CCE85789.1; -; Genomic_DNA.
DR AlphaFoldDB; G8Y521; -.
DR STRING; 559304.G8Y521; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_1_1; -.
DR InParanoid; G8Y521; -.
DR OMA; IRIRRHN; -.
DR Proteomes; UP000005222; Chromosome M.
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:UP000005222};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 629..839
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 998 AA; 112741 MW; E0FE323608FDB615 CRC64;
MLRAFRSKVT RSCLLKAQVR PQIRRFATGS DTFLQGSNGN YVDEMYDAWK QDPKSVHVSW
DAYFRNVDSG AIEPSRAFMP PPTLVPTPSG GIPGFVPGES PISEDVVTHL KVQLLVRAYQ
VRGHQMAKID PLGISYGSNT PAPKELTLEH YGFTDADMNK QITLGPGILP RFVDAGKKSM
TLKEIIDACQ KLYCDSYGVE YIHIPSKEQC DWLRERIEIP QPFKYAADEK RQILDRLIWS
CSFESFLATK FPNDKRFGLE GAESVIPGMK ALIDTSVEYG VEDVVIGMPH RGRLNMLSNV
VRKPNESIFS EFTGSKEFDE GSGDVKYHLG MNYKRPTTSG KHVNLSLVAN PSHLESEDGV
VLGKTRAIQQ YKDDLGTYKK AMSILLHGDA AFSAQGVVYE TMGFANLPAY SSGGTVHIII
NNQIGFTTDP RFARSTLYPS DIAKSINAPI FHVNADDVES CIFMCNLAAE WRATFHTDVI
IDLVCYRKYG HNETDQPSFT QPLMYKKIAE KKSVIDYYTK QLIEEGTFTA EDIDEHKKWV
WNILEESFSK SKEYEPTSRE WLTTPWEDFK SPKELATEVL PHLPTTVEEE TLKKIGKAVS
EVPKGFDLHR NLKRILNNRK KTVETGEGID WATGEALAFG SLALEGYHVR VSGQDVERGT
FSQRHAVLHD QSSEQTHTPL NHLSDSQAPF VITNSSLSEF GVMGFEYGYS LFSPDAFVMW
EAQFGDFANN AQVMIDQFIA SAESKWKQRS GVVLSLPHGY DGQGPEHSSG RIERYLQLCN
EDQRYFPAPE KLERQHQDAN MQVAYPTTPA NLFHLLRRQM HRQFRKPLIL FFSKSLLRHP
LAKSNMSEFT GDSHFQWIIE DPELDKSISS KEGIKRVVLC SGQVFTALHK KRAAIEDKTT
AFIRIEQLHP FPFAQLRDTL DTYPNLEDLV WVQEEPLNFG SYSYSAPRIA TILEQTNNHK
GLTLRYAGRD PSASIAAGTK SMHTAEEEAF LKEAFQEN
//
