ID   A0A1N6PZQ3_9GAMM        Unreviewed;       943 AA.
AC   A0A1N6PZQ3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=SAMN05421647_102146 {ECO:0000313|EMBL:SIQ09766.1};
OS   Marinobacterium stanieri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinobacterium.
OX   NCBI_TaxID=49186 {ECO:0000313|EMBL:SIQ09766.1, ECO:0000313|Proteomes:UP000186895};
RN   [1] {ECO:0000313|EMBL:SIQ09766.1, ECO:0000313|Proteomes:UP000186895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7027 {ECO:0000313|EMBL:SIQ09766.1,
RC   ECO:0000313|Proteomes:UP000186895};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-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};
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DR   EMBL; FTMN01000002; SIQ09766.1; -; Genomic_DNA.
DR   RefSeq; WP_010324262.1; NZ_FTMN01000002.1.
DR   AlphaFoldDB; A0A1N6PZQ3; -.
DR   STRING; 49186.SAMN05421647_102146; -.
DR   eggNOG; COG0567; Bacteria.
DR   Proteomes; UP000186895; 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:UP000186895};
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;  106696 MW;  E49BAC9F9232ECAA CRC64;
     MQDGIMEQMW KNAHLYGGNL SYVEQLYETY LMDPNAVPQE WREEFDKLPK VGDSISQDVP
     HSTVREHFLL LSKNQKRATP VSGSSVSSEH EKKQVRVLRM INAFRVRGHQ HADIDPLNLM
     EREQVPDLDP RFHELSEADF DTRFQLGSLF FGPEESSLKE ILADLKKTYC TTVGAEYMHI
     VDTQEKRWIQ SRMEPVRSHP VLTNEERTHI LERLSAAEGL EKYLGSRYAG AKRFGLEGGE
     SLIPCLDELV QRAGRDGAKE LVIGMAHRGR LNVLVNIFGK NPQELFGEFE GKKMLETSGD
     VKYHQGFSSN VMTAGGEVHL AMAFNPSHLE IVSPVVEGSV RARQDRRDDA IGNSVIPVSI
     HGDAAVAGQG VVMETYQMSQ TRAYKTGGTI HIVINNQVGF TTSKKEDARS TEYCTDVAKM
     VQAPIFHVNG DDPEAVRFVT QLALDYRNEF NKDVVIDLVC YRRRGHNEAD EPSGTQPLMY
     KQIKVQKTTK ELYAARLVEE GVLSAEEAKS LDQEYRQALE NGEHVAKSLV MQPNEELFVD
     WRPYLGHKWS FECDTSVDPK LLKELANKTC EFPEGFNIQR QVQKIYEDRK KMAAGAMEIN
     WGFAETMAYA TLLAEGYPIR LTGQDVGRGT FSHRHAVVHN QKDATNYVPL QNLAEGQPDF
     DIYDSFLSEE AVLAFEYGYA TTTPNALVIW EAQFGDFANG AQVVIDQFIT SGEHKWGRLC
     GLTMLLPHGF EGQGPEHSSA RLERFLQLSA EHNIQVCVPS SPAQIFHLLR RQVVRPLRKP
     LIIMSPKSLL RHKQAVCSLE DLSEGTFEPV LSEVDTLDPK KVKRLVMCSG KVYYDLYNRR
     AELEKDDVAI IRIEQLYPFP EEPLKQAIAE YTNLESVVWC QEEPMNQGAW YCSQHHMRNV
     LQQHDAKLYL EGVGRPHAAA PAVGYISVHL EQQEKLVNEA ING
//