ID   A0A430KSD5_9GAMM        Unreviewed;       943 AA.
AC   A0A430KSD5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=EH243_07520 {ECO:0000313|EMBL:RTE66435.1};
OS   Amphritea opalescens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Amphritea.
OX   NCBI_TaxID=2490544 {ECO:0000313|EMBL:RTE66435.1, ECO:0000313|Proteomes:UP000283087};
RN   [1] {ECO:0000313|EMBL:RTE66435.1, ECO:0000313|Proteomes:UP000283087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANRC-JH13 {ECO:0000313|EMBL:RTE66435.1,
RC   ECO:0000313|Proteomes:UP000283087};
RA   Fang Z., Zhang Y., Han X.;
RT   "The draft genome sequence of Amphritea opalescens ANRC-JH13T.";
RL   Submitted (NOV-2018) 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   -!- 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:RTE66435.1}.
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; RQXW01000005; RTE66435.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A430KSD5; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000283087; 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   ECO:0000313|EMBL:RTE66435.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283087};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          599..792
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   943 AA;  106733 MW;  B4AE15F21F7CA7DF CRC64;
     MQEGIMELMW KNAHLYGGNL SYIEQLYESY LMDPNAIPQE WRDEFDRLPK VGDNLTQDVP
     HSPVRDHFLY LSQHQRHSAA ANGSGNSSDH EQKQIRVLRM INAYRVRGHQ AADIDPLDLS
     KREPVPDLDP RFHELSEADF DTTFQTGSLF FGGEEATLKE ILDDLKKTYC TTVGAEYMHI
     VDTQEKRWIQ SRLEPVRSHP SVDADRKMMV LERLTAAEGL EKYLGSRFAG AKRFGLEGGE
     SLIVSLNTLI QRAGKQGARE VVIGMAHRGR LNTLVNIFGK SPTELFGEFE GKKTLETSGD
     VKYHQGFSSN VMTGGGEVHL AMAFNPSHLE ISSPVVEGSV RARQDRREDA VGTTVVPVNI
     HGDQAFAGQG VVMETFQMSQ TRAYKTGGTI HLVVNNQVGF TTNKQEDSRS TEYCTDIAKM
     VQAPIFHVNG DDPEAVRFVT QLAVDYRTEF KKDVVIDLVC YRRRGHNEAD EPSGTQPLMY
     KQIKLQKSTR ELYAQQLISE GLLTAEQSKQ LELDYRKDLE EGKHVTHSLV LEPNQELFVD
     WTPYLGHQWS FDCDTRVDNK LLQELGTKIC EVPEGFQVQR QVQKIYDDRK RMAVGAMQLN
     WGMAESLAYA TILAEGFPVR LTGQDVGRGT FSHRHAVLHD QRNGDVYEPL KNIAADQPVL
     TLHDSFLSEE AVLAFEYGYS TTMPNALVIW EAQFGDFANG AQVVIDQFIT SGEHKWARLC
     GLTMLLPHGF EGQGPEHSSA RLERYLQLCA EHNIQVCVPT TPAQMFHLLR RQIVRPLRKP
     LVVMTPKSLL RHKQAVSSLE ELSDGAFYPV IAETDTMDPK KVKRLVLCSG KVYYDLYNRR
     AELEKDDVAI IRIEQLYPFP EDQMYDAIKQ YTNLESAVWC QEEPMNQGAW YCSQHHMRHA
     LARHNDKINM EGVGRPHAAA PAVGYISVHL EQQEKLVNEA ING
//