ID A0A060SRF6_PYCCI Unreviewed; 1003 AA.
AC A0A060SRF6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=BN946_scf184657.g12 {ECO:0000313|EMBL:CDO77137.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO77137.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO77137.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO77137.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) 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:CDO77137.1}.
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DR EMBL; CCBP010000443; CDO77137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060SRF6; -.
DR STRING; 5643.A0A060SRF6; -.
DR HOGENOM; CLU_004709_1_1_1; -.
DR OMA; IRIRRHN; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000029665; 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:UP000029665};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 637..847
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1003 AA; 113538 MW; 77FB8263C248D62E CRC64;
MHRLTRLPRF IQPLSGSRYR FAISSVAPAA RTYAALAKGP SPNDAFANGT NSYYIDEMYR
LWREDPKLVH PSWNTYFSGM EKGLPSYKAF TPPPSFVPTG VANLNLTGNP DLDVHLKVQL
LVRAYQVRGH HLAELDPLGI LDPDLTDMHP PELELARYGF TERDLDTPIT LGPGILPHFA
TEDRKTMTLG EVISTLKRIY CGSIGFQYVH IPDKDKCDWI RERIEIPKPW NYTLEEKRMV
LDRLIWSESF EKFIATKYPN EKRFGLEGGE SLIPGMKALI DRSVEHGVKD ITIGMPHRGR
LNVLANVIRK PIEAILNEFS GTADEDDYHT GDVKYHLGAN YVRPTPSGKK VSLSLVANPS
HLEAEDPLVL GKTRALQHFA NDEQTHDTAM GILLHGDAAF AGQGVVYETM GFHNLLNYGT
GGTVHLIVNN QIGFTTDPRF SRSTPYPSDI AKAFDAPIFH VNGDDVEAVN FVCQLAADWR
AKWKSDVIID IVCYRRHGHN ETDQPSFTQP RMYRAIEKQP TTLTKYTKEL IDRGIFTEED
IEEHKKWVWG MLEKGAEGAK TYVPTSKEWL SSSWPGFPSP KELIEKTLPT RDTGSSEETL
KHVGKVISSF PEGFHPHRNL ARILTNRGKT IEEGKNIDWA TAEALAFGSL ALEKIHVRLS
GQDVERGTFS QRHAVIHDQE NEQQYVPLNN LGGGQARFVV CNSSLSEYGA LGFELGYSLV
SPDALTIWEA QFGDFANNAQ CIIDQFIASG ERKWLQRTGL VVNLPHGFDG QGPEHSSGRL
ERFLQLCDDH PHIFPTPEKI ERQHQDCNMQ VVYPTTPANY FHVLRRQIHR DFRKPLILFF
SKSLLRHPRA RSDLSEMVGD THFLRYLPEP HPENLVAPEK IRRHILCTGQ VYHTLLQHRE
EQGINDVAIS RLEQISPFPY DLLTPHLDKY PNADLLWCQE EPLNNGAWSY VGPRIRTAAN
ETKHHKGKYP LYAGREPTSS VATGSKALHK KQIEMFLADA FKQ
//
