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Database: UniProt
Entry: A0A068RKW6_9FUNG
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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
//
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