ID   A0A2G5K829_9RHOB        Unreviewed;       983 AA.
AC   A0A2G5K829;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=BFP76_00705 {ECO:0000313|EMBL:PIB25687.1};
OS   Amylibacter kogurei.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Amylibacter.
OX   NCBI_TaxID=1889778 {ECO:0000313|EMBL:PIB25687.1, ECO:0000313|Proteomes:UP000231516};
RN   [1] {ECO:0000313|EMBL:PIB25687.1, ECO:0000313|Proteomes:UP000231516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4G11 {ECO:0000313|EMBL:PIB25687.1,
RC   ECO:0000313|Proteomes:UP000231516};
RA   Wong S.-K., Hamasaki K., Yoshizawa S.;
RT   "Draft genome of Amylibacter sp. strain 4G11.";
RL   Submitted (AUG-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:PIB25687.1}.
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DR   EMBL; MDGM01000009; PIB25687.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5K829; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000231516; 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:UP000231516};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          627..821
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   983 AA;  110411 MW;  AECD590D782D6DCE CRC64;
     MNEQPSNDQF HALSFLQGHN AEYIEQLYAQ YVANPSSVDA SWQAFFAELG DDVDAVTAEA
     TGATWKRPDW PPAPNDELIA ALDGQWGEDP QKAGEKIKSA AAGKGVTLSD ADVQKAVLDS
     MRALMIIRAY RIRGHLIAAL DPLDMRSKEP HPELDPKFYG FQETDMDRPI FLDKVLGMET
     ASMRQILAKL RKTYCGTFAL QYMHLSDPEE AGWLKERIEG YEHESFFTTQ GRRAILNKMV
     EAEGFEKFCH VKYSGTKRFG LDGGEALIPA MEQIIKRGGA LGVKDIIVGM PHRGRLNVLC
     NVMSKPYRAI FNEFLGGSYK PDDVEGSGDV KYHLGASADR EFDGNSVHLS LTANPSHLEA
     VNPVVLGKAR AKGDQLGRDR GAVLPVLLHG DAAFAGQGVV AECFGLSGLK GHITGGTMHI
     VVNNQIGFTT SPHDSRSSPY PTDIAMMVEA PIFHVNGDDP EAVVHAAKIA TEFRQKFRKD
     VVLDIFCYRR FGHNEGDEPM FTQPTMYKKI KAHKTSLTIY TERLVREGLI PEGEIEDMKT
     AFQMRLNEEF EAGKVYKPNK ADWLDGRWSH MKSKDPEYQR GKTHISKKRF KEVGEALTRL
     PEKWTPHRTI QRILDAKAEM IKSGKGIDWA TGEALAFGTL QVEGFPVRLS GQDCTRGTFS
     HRHSGILDQN TGEKFYPLNN IRDDQEGHYE VIDSMLSEYA VLGYEYGYSL AEPNALTLWE
     AQFGDFANGA QIMFDQFISS GESKWLRMSG LVMLLPHGME GQGPEHSSAR PERFLQMCAE
     DNWVIANVTT PANYFHILRR QLHRTYRKPL VIMTPKSLLR HKLAVSTIDD FTGDSSFHRV
     LWDDAQLGNS DTKLKADKDI KRVVICSGKV YYDLLEERDA RGIDDIYLLR FEQLYPYHDA
     AAKVELKRFK NAEFIWCQEE PKNQGYWDFI NPRIEETLVD LGMKNNRPKY VGRPSAAAPA
     TGLASQHKKQ QAALVNDALT LKG
//