ID A0A1B6YMG3_9RHOB Unreviewed; 987 AA.
AC A0A1B6YMG3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN ORFNames=A8B83_14480 {ECO:0000313|EMBL:OAN70019.1};
OS Rhodobacteraceae bacterium EhC02.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1849170 {ECO:0000313|EMBL:OAN70019.1, ECO:0000313|Proteomes:UP000078223};
RN [1] {ECO:0000313|EMBL:OAN70019.1, ECO:0000313|Proteomes:UP000078223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhC02 {ECO:0000313|EMBL:OAN70019.1,
RC ECO:0000313|Proteomes:UP000078223};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC dehydrogenase); the complex contains multiple copies of the three
CC enzymatic components (E1, E2 and E3). {ECO:0000256|ARBA:ARBA00011301}.
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:OAN70019.1}.
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DR EMBL; LXYH01000020; OAN70019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B6YMG3; -.
DR STRING; 1849170.A8B83_14480; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000078223; 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 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000078223};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 631..824
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 987 AA; 110786 MW; F103A517E57A17D2 CRC64;
MTEQSPNDVF HASSFMQGHN AEYLEQLYAR YAADPNAVDE AWQAFFRAMG DADHDVKREA
AGPSWARADW PPAPSDELTS ALDGQWPAPV ETRAAGQKIA AKAAEVGVKV TDDQVKRAVL
DSVRALMIIR AYRIRGHLAA DLDPLGLREP TPHPELDPKS YGFTEADMDR PIFIDNVLGL
QIASMRQILD IVKRTYCGTF ALQYMHISDP EQSAWLKERI EGYGKEITFT REGRRAILNK
LVEAEGFEKF LHVKYMGTKR FGLDGGESLI PAMEQIIKRG GNLGVKEIVI GMPHRGRLSV
LANVMGKPYR AIFNEFQGGS FKPEDVDGSG DVKYHLGASS DREFDGNEVH LSLTANPSHL
EAVNPVVLGK VRAKQAQMND TDRSKVLPVL LHGDAAFAGQ GVVAECFALS GLVGHKTGGT
MHIVVNNQIG FTTAPHFSRS SPYPTDNALV VEAPIFHVNG DDPEAVVHAA KVATEFRQMF
HKDVVLDIIC YRRFGHNEGD EPMFTNPVMY NKIKKQKTTL TLYTERLVKD GLIPEGEIED
MKAAFQARLN EEFEAGKDYK PNKADWLDGR WSHLDRRDQK KYQRGKTAIK PETMEQIGTA
LTRAPEGFPM HKTVERLLET RKKMFDTGEG FDWATGEALA FGSLLLEGYP VRLAGQDSTR
GTFSQRHSAL INQDTEERYY PLNNIREGQA RYEVIDSMLS EYAVLGFEYG YSLSEPNALV
MWEAQFGDFA NGAQIMFDQF ISSGESKWLR MSGLVCLMPH GYEGQGPEHS SARLERFLQM
CGQDNWIVAN CTTPANYFHI LRRQLHRTFR KPLMLMTPKS LLRHKMAISD AADFTTGSSF
HRVLWDDAEK GHSDTKLAAD DKIKRVVMCS GKVYYDLLEE RDARGIDDIY LLRIEQFYPF
PAMSLVRELE RFKDAEMVWC QEEPKNQGAW SFIEPNIEWV LGRIDAKHQR PVYAGRAASA
SPATGLASTH KAQQQALVDE ALTIKGK
//
