ID A0A1V9Z1F0_9STRA Unreviewed; 1023 AA.
AC A0A1V9Z1F0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=ACHHYP_04301 {ECO:0000313|EMBL:OQR91839.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR91839.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR91839.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR91839.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQR91839.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JNBR01000498; OQR91839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9Z1F0; -.
DR STRING; 1202772.A0A1V9Z1F0; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000243579; 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:UP000243579};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 641..866
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1023 AA; 114564 MW; 9542BFD6D082BFF7 CRC64;
MAQWSKLAAA SRVLRRSVAT PMKTGMRSFA SAPHPSESFI NGTNNVYVEE MYRSWTADPS
SVHKSWDVYF RQVDAGAVPG EAFIPPPTVQ TGVTPVVRGA AASSPLGINH ALGLSYLIRA
YQSRGHENAN LDPLGLQERP VLPELDIKMY GFTEADLDKT IDIPKNFASG VTGFLEELTE
GKNPTLGQIV QRLQETYCNS IGVQYMHIPD REKCNWIRTK LEHLVKKEET KEKKMHILER
LAFSVNFERF LGNKYNTTKR FGLDGGESLI PGLKYMIDRA TEMGMEHVVV GMPHRGRLNV
LANVIRKPIQ QIFKEFQGTH FDLDKYVNDV EDWSNSGDVK YHLGTSFDRT YPDGRKVHLS
LVANPSHLEA VNPVVEGKVR AKQFYLGNDD DAEKKVMPLL LHGDAAFSGQ GVVYETMHLS
ELENYDTGGT VHVVVNNQIG FTTDPKNSRS SQYCSDVGKA MNVPIFHVNG DDPVAVVKVF
ELAAEWRQTW RSDVIINLTC YRKFGHNEID NPFFTQPLMY KKIGAMPSVL DKYAGELVAS
GVASKEETDA VVSKVWDFFA RTFEESKNWE DSKKSDWLAN RWESFKSPTQ QSRIRPTGVE
VDTLKKIGDK LTTIPDGFEL NSQLKRIIAT KRTSIETGEG LDWSSGEALA WGSLLLEGNH
VRISGQDVER GTFSHRHAVL HDQKTNDEFV PLNTLAPSLD PSAPLVNTGG NSQAPFVASN
SSLSEFGVLG FELGYSLENP NALVMWEAQF GDFANGAQII IDQFLSAGED KWMRQSGLVM
LLPHGYEGQG AEHSSCRIER FLQQTDDDPN VVPPMDEDHR MQIQQTNWQI VYCSTPAQYF
HVLRRQLHRE FRKPLISVQP KSLLRLKQAS SSLAEMGPGT KFHRVLGDSA ALVADNKVKR
VLFCSGKVYY DLAAEREAHN IDDVAIVRVE QIAPFPFDKV AEFAAKYPNA DIKWVQEEPE
NMGFWTYVSP RFETALKTIN GDSRRPTYVG RVASAAPATG YHAVHNLEQS RIISKALDLP
KTN
//
