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
//
