ID   A0A2A5BGC1_9GAMM        Unreviewed;       705 AA.
AC   A0A2A5BGC1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-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};
DE   Flags: Fragment;
GN   ORFNames=COA99_18155 {ECO:0000313|EMBL:PCJ30430.1};
OS   Moraxellaceae bacterium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae.
OX   NCBI_TaxID=1889775 {ECO:0000313|EMBL:PCJ30430.1, ECO:0000313|Proteomes:UP000218379};
RN   [1] {ECO:0000313|Proteomes:UP000218379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) 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:PCJ30430.1}.
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DR   EMBL; NVVG01000255; PCJ30430.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A5BGC1; -.
DR   Proteomes; UP000218379; 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; 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; 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; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 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          12..49
FT                   /note="2-oxoglutarate dehydrogenase E1 component N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16078"
FT   DOMAIN          227..529
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
FT   DOMAIN          600..700
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02779"
FT   NON_TER         705
FT                   /evidence="ECO:0000313|EMBL:PCJ30430.1"
SQ   SEQUENCE   705 AA;  78607 MW;  57674F6A1E557EE4 CRC64;
     MEDSLMYRQW STSHLSGGNA VYVEELFESY LKDPNSVPED WRQNFDKLPL VAGAESDVPH
     STIVEHFLFL AKNKNRAQPV AVSSVSTEHE RKQVQVLQLI TAYRVRGHQN AILDPLSLME
     RAHVPDLELA HHGLSAADID TLFQTGNLFI GKDEASLGVI VEALRKTYCA SVGVEYMHIV
     DTAEKRWIQQ RMESVRSKPN YSLEVKSHLL ERISAAEGLE KMLATKYPGT KRFGLEGGDS
     LIPCVDELIQ RCGSYGVKEI VIGMAHRGRL NVLVNTLGKN PATLFDEFEG NHQMNTDGSG
     DVKYHQGFSS NVMTPGGEIH LALAFNPSHL EIVSPVVEGS VRARQDRRGD LNGDLVVPIL
     IHGDAAFAGQ GVVMETFQMS QTRGFKTGGT VHIIVNNQVG FTTSEQEDAR STEYCTDIAK
     MVQAPIFHVN GDDPEAVLFV TQMAIDFRTQ FKKDVVIDII CYRSRGHNEA DEPSITQPMM
     YQVIRSKKSP RQLYAAQLVA EGAMTQEETD RVVDDYRNAL DDGLHVAKSL VKEPNSKLFV
     DWTPYLGHSY DAYYDTSVDY KKLQELAQKL TTVPEGFVVQ RQVNKIIEDR KKMAAGALMV
     DWGFAENLAY ATLLDAKFPV RLTGQDVGRG TFSHRHAVFH NQKEAGRYIP LESIADEDTA
     MDIYDSLLSE EAVLGFEYGY ATTSPEGLVI WEAQFGDFVN GAQIM
//