ID A0A1G3HPG0_9RHOO Unreviewed; 942 AA.
AC A0A1G3HPG0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=A3H93_12240 {ECO:0000313|EMBL:OHC70305.1};
OS Rhodocyclales bacterium RIFCSPLOWO2_02_FULL_63_24.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales.
OX NCBI_TaxID=1802018 {ECO:0000313|EMBL:OHC70305.1, ECO:0000313|Proteomes:UP000178519};
RN [1] {ECO:0000313|EMBL:OHC70305.1, ECO:0000313|Proteomes:UP000178519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- 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:OHC70305.1}.
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DR EMBL; MHZX01000069; OHC70305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3HPG0; -.
DR Proteomes; UP000178519; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 595..792
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 942 AA; 105230 MW; D427156532B90A20 CRC64;
MMKQMLSNSY LFGTNTPYIE ALYDAYLANP AAVEPAWRDY FDKLGTLPGA GNYTGPDVAH
YPIITSFAQR AKEGTLQASS RAAMSDGKQV KVLQLINAYR FLGNRWAQLD PLKRSERPAI
PELEPSHYGF TEADLGQVFQ TGSFAAVPES ATLREILEAS RQTFCGTIGA EFMYLSDVGQ
KRWLQGKLEP IRATPAYSAE DKKRFLVQLT HAETLERYLH TKYVGQKRFS LEGGEALIVA
MDQLIRTAGT VGVQEMVIGM AHRGRLNVLV NTLGKQPAML FDEFEGKKKS ALSAGDVKYH
MGYSSDVGTP GGPVHLTLAF NPSHLEIVNP VVAGSVYARQ VRRGADGKKQ ALPVLIHGDA
AVAGQGVNQE MLNFSNTRGY GTGGTVHIVV NNQIGFTTSD LRDYRSSLYC TDIFKMIEAP
IFHVNGDDPE AVALVTQIAM EYRQEFKKDV VIDIVCFRKL GHNEQDEPMV TQPLMYKKIA
QHPGTRKLYA DKLAAQGVIA AGDAEQMIKD YRAALDEGRH LIDPVISDYH SKFSIDWTPY
IDVPYTEKCD TTVSTAELQR LAKRLTDIPA NFTLHSRVQK IIDDRKQMGE GKLPVDWGMG
ENLAYATLVA AGFNIRVSGE DVGRGTFFHR HAALHDQNRE KWDEGTYWPL QNIQEHQGRF
MCFDSVLSEE AVLAFEYGFA TAAPNEMVVW EAQFGDFANG AQVVIDQFLS SGEAKWGRGC
GLVLLLPHGY EGQGPEHSSA RLERYMQLSA EFNWEVCVPT NAAQIYHMLR RQMLRKQRKP
LVVMTPKSLL RHKDATSSMD DLANGTFQTI IGEIDKVEAK KVTRMVTCAG KIYFDLLAER
RAKKIDHIAL VRVEQLYPFD DRRLAEEMKK YPNLKELVWC QEEPENQGAW YAKHHRLTEL
IKKGQTLSVV ARPASASPAV GYAAKHTLQQ KEVVNAALGI KE
//
