ID C5PG54_COCP7 Unreviewed; 1063 AA.
AC C5PG54;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=CPC735_048770 {ECO:0000313|EMBL:EER23507.1};
OS Coccidioides posadasii (strain C735) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=222929 {ECO:0000313|EMBL:EER23507.1, ECO:0000313|Proteomes:UP000009084};
RN [1] {ECO:0000313|EMBL:EER23507.1, ECO:0000313|Proteomes:UP000009084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C735 {ECO:0000313|Proteomes:UP000009084};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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:EER23507.1}.
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DR EMBL; ACFW01000049; EER23507.1; -; Genomic_DNA.
DR RefSeq; XP_003065652.1; XM_003065606.1.
DR AlphaFoldDB; C5PG54; -.
DR GeneID; 9691122; -.
DR KEGG; cpw:CPC735_048770; -.
DR VEuPathDB; FungiDB:CPC735_048770; -.
DR HOGENOM; CLU_004709_1_0_1; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000009084; 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 ECO:0000313|EMBL:EER23507.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 687..897
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1063 AA; 120011 MW; 501CA2313484CAB2 CRC64;
MLRATRSSSS KVSEVAGLLR KTPYVRNARC IASSSKPTSL SARANFGLAT RRPLALVAAQ
EAWKQRRQYA IAAEETNKGV DPNDSFLQGN TADYIDEMYL AWRKDPSSVH ISWQTYFHNI
EEGNMPISQA FQPPPTLVPT PTGGVPQHMP TSRTAAGAEV SNHLKVQLLV RAYQARGHHK
AKIDPLGIRG EAESFGYSKP KELELEHYGF TEADLDQEFA LGPGILPRFE TETRKKMTLR
EIIGACERIY CGSFGIEYIH IPDRGPCDWI RDRVEIPQPY KYSVDEKRRI LDRLIWSTSF
EAFLATKFPN DKRFGLEGCE TLVPGMKALI DRSVDYGIKD IVIGMPHRGR LNVLSNVVRK
PNESIFSEFT GTAEPSDEGS GDVKYHLGMN FERPTPSGKR VQLSLVANPS HLEAEDPVVL
GKTRAIQHYN NDEKNFNSAM GVLLHGDAAF AAQGIVYETM GFHSLPAYST GGTIHIIVNN
QIGFTTDPRF ARSTPYCSDI AKAIEAPVFH VNADDVEAVN FVCQLAADWR AQFKSDVVID
IVCYRKQGHN ETDQPAFTQP LMYKRIADQT TQLDKYVNKL LQENTFTKED IEEHKKWVWG
MLNDSFDRSK EYQPTSREWL TSAWNGFKSP KELATEVLPH LPTGVSRDTL RMIGDKIGET
PQGFSVHRNL KRILANRKKT VDEGNNIDWA TAEALAFGTL CNEGHHVRVS GQDVERGTFS
QRHAVLHDQQ NEATYTPLQH ISENQGTFVI SNSSLSEFGV LGFEYGYSLT SPNALVMWEA
QFGDFANNAQ CIIDQFIASG EVKWLQRSGL VMSLPHGYDG QGPEHSSGRL ERYLQLSNED
PRVFPSPDKI DRQHQDCNMQ IAYMTTPSNL FHILRRQINR QFRKPLVIFF SKSLLRHPLC
RSSIEEFTGD SHFRWIIPET EHGKSIAEPE KIERVILCSG QVWAALVKHR DANGIKNTAI
TRIEQLNPFP WQQLKENLDS YPNAKDIVWC QEEPLNAGAW SFVQPRIETL LNNTEHHNRR
HVLYAGRNPS ASVATGLKAS HIKEEQELLQ DAFTVHQDKL KGE
//
