ID   A0A0C9MBE4_9FUNG        Unreviewed;       942 AA.
AC   A0A0C9MBE4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=2-oxoglutarate dehydrogenase, E1 component {ECO:0000313|EMBL:GAN07911.1};
GN   ORFNames=MAM1_0182c07416 {ECO:0000313|EMBL:GAN07911.1};
OS   Mucor ambiguus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN07911.1};
RN   [1] {ECO:0000313|EMBL:GAN07911.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN07911.1};
RA   Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT   "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT   ambiguus NBRC6742.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; DF836471; GAN07911.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9MBE4; -.
DR   STRING; 91626.A0A0C9MBE4; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000053815; 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; 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:UP000053815};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          586..791
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   942 AA;  106108 MW;  27EF79525509B499 CRC64;
     MFRLSSLTKN TNHRRSTTTL LRQGARRSYH DDGVYGYRVA KEFKLPDYTA EELSNRMKYG
     SLLRMVQAYR THGHEGAHLD PLNIMKRKEV LALKPERYGL GEHASESYNL AGILHVNDAM
     QERTLGNEAD FKTILDHLQA VYCGKIAYEF MHLPSASERR WWYHAVESWE KPQLDVEQKK
     RIHEILSKSE VFDQFLGKKF PNLKRYGLEG AESMMVALDR LFELSAKNNI QDIVIGMPHR
     GRLNLLCDLL QYPYAALFHK MKGHSELPEG VFGSGDVISH LVNNPDLTYA GNKVHVSLLA
     NPSHLEAINP VAMGKARAKQ AGLLASSDET CNLGDRVMCV QIHGDAAFAG QGIVMEGLGM
     SNLAHYSSGG SVHIVVNNQL GYTTPAQNAR SSAYCSDIGK MINVPVVHVN GDFPEDVARA
     LDMVFEYRNK FRKDIILDLM CYRRWGHNEL DEPAFTQPVM YNNIRHRTSV PKLYEKKLID
     EQTLSSAEEA QQVRESQVKQ LEQGLQDAEN FVPDAEHFHL DKNWKGLHHI TTGSESETPD
     TGCDESVLAE IGLLSVTPPD NVKVHSRLQK YHIDQRTKKL KQGNGLDWAT AEALAFGSLI
     QEGYDVRISG QDVGRGTFSQ RHAMFVCQDT ERAVVPLNHM QSDQKNFLEV ANSPLSEFAV
     LGFEYGMSIE SPKRLVLWEA QFGDFFNGAQ ITIDTFLSSG EEKWMRQSGL VMLLPHGQDG
     AGPEHSSSRV ERFLQMSNDA FDVNKVQDRP PNWHIVNCTT PAQYFHVLRR QMLRSYRKPL
     IVISPKSLLK SPLAVSSLAD MAPGTCFQPV LKDASIKNDA QVEKVVFLSG KFYYDLVKER
     QTRGLDDKVA LIRIEELSPF PKDALAKEIQ KYAGAREFVW CQEEPQNAGA YAFMAPRLAQ
     LLPENKAIQY VGREPLSAPA VGISSVFKKQ AQELLQKSML IN
//