ID A0A0K3C5I8_RHOTO Unreviewed; 966 AA.
AC A0A0K3C5I8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=BY PROTMAP: gi|472581982|gb|EMS19690.1| oxoglutarate dehydrogenase (Succinyl-transferring) [Rhodosporidium toruloides NP11] gi|647395031|emb|CDR36267.1| RHTO0S01e17898g1_1 [Rhodosporidium toruloides] {ECO:0000313|EMBL:CTR04949.1};
DE SubName: Full=Dehydrogenase E1 and transketolase domain-containing protein 1 {ECO:0000313|EMBL:PRQ78206.1};
GN Name=FGENESH: predicted gene_1.810 {ECO:0000313|EMBL:CTR04949.1};
GN ORFNames=AAT19DRAFT_9274 {ECO:0000313|EMBL:PRQ78206.1}, BN2166_0008100
GN {ECO:0000313|EMBL:CTR04949.1};
OS Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR04949.1, ECO:0000313|Proteomes:UP000199069};
RN [1] {ECO:0000313|EMBL:CTR04949.1, ECO:0000313|Proteomes:UP000199069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Single colony {ECO:0000313|EMBL:CTR04949.1};
RA Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PRQ78206.1, ECO:0000313|Proteomes:UP000239560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 0880 {ECO:0000313|EMBL:PRQ78206.1,
RC ECO:0000313|Proteomes:UP000239560};
RX PubMed=29521624;
RA Coradetti S.T., Pinel D., Geiselman G., Ito M., Mondo S., Reilly M.C.,
RA Cheng Y.F., Bauer S., Grigoriev I., Gladden J.M., Simmons B.A., Brem R.,
RA Arkin A.P., Skerker J.M.;
RT "Functional genomics of lipid metabolism in the oleaginous yeast
RT Rhodosporidium toruloides.";
RL Elife 7:0-0(2018).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CWKI01000001; CTR04949.1; -; Genomic_DNA.
DR EMBL; LCTV02000001; PRQ78206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K3C5I8; -.
DR STRING; 5286.A0A0K3C5I8; -.
DR OMA; TPAQYYH; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000199069; Unassembled WGS sequence.
DR Proteomes; UP000239560; 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 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; 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; 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:UP000199069};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 604..816
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 100..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 107215 MW; 715FD11399A25A81 CRC64;
MLRSSLRIRP RPHALLSQTH RRSLHDRGIW GYEEPKTYTL PDFTPSELAN RSQNASLLRL
VESYRRHGHR AALVDPLDLA QRPVVPALDP RRYGLGAEPE RDEFVSETLA ETGEDEGKKY
DTTGILDFPE DGKGSMRTMK EISQRLAEVY CGGVAYEFMH MPSKHERRFL ETLLERSHAE
PISASEQLEN WRLLARSEGF DQWAAKRFPN VKRYGGEGAE SMMVAAAKIL GEATKGGVED
VVIGMPHRGR LNLLTQLLSL DMRLLVRKMR GLPTLPPSLP PSQFTDDVLS HLFLSTRYTP
PSSSDSLTVH LLPNPSHLET VTPVALGFAR GLQVPFGSLE AQKSGSSQPY ELGSKVLSLS
IHGDAAFGGQ GVVAESLNLA SLPHFTCGGT VHIVVNNQIG YTTPATQGRS SFYATDLAKM
IAAPVLHVNG DKVDDVARAM KLALAYQQKF KKDVVIDLVV YRRRGHNELD EPAFTSPVMY
SKIKDLPSVA QLYEQHLVSQ STLSSSDAAS YRKSHFASLD EALAAADPEK FTPPELEMPR
GWAEMRWPKE GEWETQVDTG YDQQVLREIG ERSVQVPDEI TIHPRLLKMH IRKRLDSLKE
GAGIDFATAE ALAFGSLLLE GNHIRLCGQD SGRGTFSQRH AILADQTSER VAVPLQTLTS
SPPSSSSSST QPGTIEVVNS PLSEYAPLSF EQGLAYVSPK MLPIWEAQFG DFHNTAQVTI
DTYLGGGETK WGMQSALTLL LPHGQDGAGP EHSSSRIERF LQLTNEPLSR SKPFVPNMHL
VNVTTAAQYF HLLRRQMKRD YRKPLVVFSP KGILRLPAAS SRLAEMAPGT TFQPVLTEQV
ADPSTVERVV LLSGKMYFEL AKQRAERKLD GQIVFIRVEE ISPFPYKAFS DALAPFPSAK
SIAWAQDEPE NAGAYLFVLP RLQQILPRGL ELEYIGRDAM ATPAPGVKKY FEEQRKDIEE
RIFAGL
//
