ID A0A068RKW6_9FUNG Unreviewed; 1043 AA.
AC A0A068RKW6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=LCOR_02003.1 {ECO:0000313|EMBL:CDH50287.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH50287.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH50287.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-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:CDH50287.1}.
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DR EMBL; CBTN010000006; CDH50287.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068RKW6; -.
DR STRING; 1263082.A0A068RKW6; -.
DR VEuPathDB; FungiDB:LCOR_02003.1; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000027586; 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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 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:UP000027586};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 662..872
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 985..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 117962 MW; 1703A789B32399B6 CRC64;
MYRAVNMGSG ISRFIRPTSL TKHYHARPLA VPATTLTRVT SASIHRLSSR PFTSSTSTHN
NNDSFLEGNG ASYIEEMYEA WLKDPNSVHL SWQVYFKNMK HGVPPSQAYS PPPTLVPSGS
ARLPKLPNEV VANASDTDIL DHMKIQLMVR AYQVRGHHIA HLDPLGILQA DLQEGSPPEL
SYQFYGFTEK DLDRTFSLGP GILPGYESVD KKMTLREIIQ HLKKIYCGSI GTEYIHIPDR
AQCDWIRSRI ETPTPYHYNV EQKKVIYDRL TWSDSFERFV ASKYPSEKRF GLEGGETLIP
GMKAMIDRAV DLGVESIVIG MPHRGRLNVL SNVVRKPNES IFCEFSGALE PSEEGSGDVK
YHLGMNYVRP TPSGKRVHLS LVANPSHLEA VDPVVLGKTR ALQYYSNDHD RNHSMAILMH
GDAAFAGQGV VYETMGFHDL PAYTTGGTVH IVVNNQVGFT TDPRFGRSTP YCTDIAKSIG
APVFHVNADD AEAVIFVMQL AADWRQTFHR DVVIDLVCYR RHGHNETDQP MFTQPKMYQA
ISKQSPVAQI YAEQLKKEGS LDDKEITDIK ERVWQLLEES YARSKDYTPT SREWLSSSWP
GFKSPKELAE EILPHYPTGV PYETLQHIGA ALTAIPENFN VHRNLKRILQ NREKAIKAGK
EIDWATAEAL SWGSLLVEGK HVRVSGQDVE RGTFSQRHAV LHDQKNERTH TLLNSISPEQ
GYLSISNSSL SEYGVLGFEL GYSLVDPNAL VIWEAQFGDF ANGAQIITDQ FIAAGEQKWL
QRTGLVLQLP HGYDGQGPEH SSARIERYLQ LCDDNPYVYP SPEKLARQHQ DCNMQVVYAS
TPAQYFHVMR RQINREFRKP LILAFSKSLL RHPMARSTLE DMSGDTHFHL YLPDPHPDHL
ESPDKIKKHI LCTGQVYYAL LRARDQNKLS DIAISRVEQP NPFPYEQVKE HVDKYPNAEI
IWCQEEPLNM GTWQHVGPRI DLSLSQSQHH SGKNVKYTGR EPSASVATGN KKRHFQEEYE
FLSWALLGEP QQPKEVSSGV PVW
//