ID M3HG11_CANMX Unreviewed; 997 AA.
AC M3HG11;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=G210_3590 {ECO:0000313|EMBL:EMG46177.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG46177.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG46177.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) 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:EMG46177.1}.
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; AOGT01002092; EMG46177.1; -; Genomic_DNA.
DR AlphaFoldDB; M3HG11; -.
DR STRING; 1245528.M3HG11; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_0_1; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000011777; 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: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:UP000011777};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 635..845
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 997 AA; 112229 MW; 651B736708111242 CRC64;
MLRAFRSAIP RAQLLKAQST IPKTSFIQIS QRFLATDSFL QGNNSNYVDE MYDAWRQDPS
SVHASWNAYF KNIERDNVEP SKAFQAPPTI VPTVSGGAAG FVPGQNPHSE DVVTHLKVQL
LVRAYQVRGH QKAKIDPLGI SFGDNANTPK ELTLDYYGFS EADLDKQITL GPGILPRFAQ
DGKKSMTLRE IIDDCEKTYC SSYGVEYIHI PSKEKCDWLR DRIEVPQPFK YSPDQKRQIL
DRLIWATSFE SFLSSKFPND KRFGLEGAEA VVPGMKSLID TSVEYGVEDV VIGMPHRGRL
NMLSNVVRKP NESIFSEFTG SKEFDEGSGD VKYHLGMNYA RPTTSGKHVN LSLVANPSHL
EAEDGVVLGK TRAIQQFKDD IGSYKKAMAV LLHGDAAFAG QGVVYETMGF ANLPAYSTGG
TIHVIVNNQI GFTTDPRFAR STLYPSDIAK GIDAPIFHVN ADDVEACTFV FNLAAEWRAT
FHTDVIIDVV GYRKYGHNET DQPAFTQPVM YQEIGKKKSV IDIYEQQLVK EGTFSAEDIQ
EHKKWVWDIL EDNFKKSKEY KPTSREWLTT PWEDFKSPKE LATEVLPHLP TAVDEATLKK
IGVAISETPE GFEVHRNLKR ILNARKKSVE TGEGIDYATG EALAYGSLAL EGYHVRVSGQ
DVERGTFSQR HAVLHDQNSE STWTPLSNLE EKQGAFNISN SSLSEYGVLG FEYGYSLTSP
DALVEWEAQF GDFANTAQVV IDQFIAGAES KWKQRSGVVL SLPHGYDGQG PEHSSARIER
YLQLCNEDQR FFPSPEKLER QHQDCNMQVA YPTTPANVFH LLRRQMHRQF RKPLILIFSK
SLLRHPLARS NLSEFTGDSH FQWIIEDVLG EKSEVKRVVL LTGQLYAALH KKRASLDDKS
TAFIKIEQLH PFPYAQLRDA LNEYPNIEDL VWAQEEPLNM GAYNFAAPRI EAVLQETEKY
KDLKLRYAGR DPSASVAAGS KAMHVVEEEQ ILTETFQ
//
