ID   A0LAA2_MAGMM            Unreviewed;       981 AA.
AC   A0LAA2;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 85.
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   OrderedLocusNames=Mmc1_2395 {ECO:0000313|EMBL:ABK44895.1};
OS   Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetococcus.
OX   NCBI_TaxID=156889 {ECO:0000313|EMBL:ABK44895.1, ECO:0000313|Proteomes:UP000002586};
RN   [1] {ECO:0000313|Proteomes:UP000002586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1
RC   {ECO:0000313|Proteomes:UP000002586};
RX   PubMed=19465526; DOI=10.1128/AEM.02874-08;
RA   Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA   Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT   "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT   coccus strain MC-1.";
RL   Appl. Environ. Microbiol. 75:4835-4852(2009).
RN   [2] {ECO:0000313|EMBL:ABK44895.1, ECO:0000313|Proteomes:UP000002586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1
RC   {ECO:0000313|Proteomes:UP000002586};
RX   PubMed=22581902;
RA   Bazylinski D.A., Williams T.J., Lefevre C.T., Berg R.J., Zhang C.L.,
RA   Bowser S.S., Dean A.J., Beveridge T.J.;
RT   "Magnetococcus marinus gen. nov., sp. nov., a marine, magnetotactic
RT   bacterium that represents a novel lineage (Magnetococcaceae fam. nov.;
RT   Magnetococcales ord. nov.) at the base of the Alphaproteobacteria.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2012).
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}.
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DR   EMBL; CP000471; ABK44895.1; -; Genomic_DNA.
DR   RefSeq; WP_011714015.1; NC_008576.1.
DR   AlphaFoldDB; A0LAA2; -.
DR   STRING; 156889.Mmc1_2395; -.
DR   KEGG; mgm:Mmc1_2395; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000002586; Chromosome.
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:ABK44895.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002586};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          616..809
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   981 AA;  110942 MW;  5190FA46828681BE CRC64;
     MAGQLDALLN GTNALYISEL YARYLDNPHA VDATWATTFG ELTEDETPEI FKEIRGASWS
     KLESGILGKP LERDPDSQTR HAHFVQGVTQ VAGTEPEQIR RATLDAIRAL MMIRTYRVRG
     HLIANFDPLG LEAREHHPEL DPANYGFAEE DMDRPIFIDY VLGLETATLR QIVRLLKETY
     CGTIGVEFMH IQEPEEKAWV QRRIESIRNR THFTLKGKRT ILQRLSESEG FETFLQLKYT
     GTKRFGLDGG ESLIPAIEQI LKRGTQLGLK EVVIGMAHRG RLNVLANIMR KPYAAIMHEF
     QGGSNKPDDV QGSGDVRYHL GASADRVFDD KKVHLSLTAN PSHLELVNPV VLGKVRAKQL
     QRGDTSQQQV MGLIMHGDAA FAGQGLVPES LALSGLKGYQ TGGTIHLIVN NQIGFTTNPR
     NSRSSPYPSD VAKMIQAPIF HVNGDDPEAV VHAARIAIEY RQAFSKDVVI DMWCYRRHGH
     NEGDEPSFTQ PIMYRAIANH PTTRQVYAQK LEREGVLKEG EGEQIYKEFH NELETSFQEA
     QYFLPTSADW LDGMWKGVSN LRGEEEMHQH KTCVPERTLR EVGKALYTPP QDFAVHRKII
     RQLRSKEQMF ESGEGFDWAT GEALAFGTLL VEGIPVRLSG QDCGRGTFSQ RHSVLIDQND
     ESRYEPLNHI RSLQADYEVI DSPLAEASVL GFEYGYASAD PHALVLWEAQ FGDFVNGAQM
     IIDQFISSGE SKWLRLNGMV MLLPHGFEGQ GPEHSSARPE RFLQLCAEDN LQVCNLTTPA
     NYFHALRRQN HRNFRKPLVI FTPKSLLRHK LCVSKLEAFI SGSSFQRVYD EVDTLVADEA
     VKRVVLCSGK VYYELLQTRR EQGSNDVAIV RIEQLYPWPR NALFKVLQRY ANAEIVWCQE
     EPANMGYWSF LFQRLIHLLE DLQSKQRLPI YAGRGASASP ASGLASKHLQ EQTHLVHEAL
     FVPLTEIPQP FRRKETVPVE K
//