ID   J7Q8Y6_METSZ            Unreviewed;       995 AA.
AC   J7Q8Y6;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
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   Name=sucA {ECO:0000313|EMBL:CCJ07442.1};
GN   OrderedLocusNames=BN69_1991 {ECO:0000313|EMBL:CCJ07442.1};
OS   Methylocystis sp. (strain SC2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylocystaceae; Methylocystis.
OX   NCBI_TaxID=187303 {ECO:0000313|EMBL:CCJ07442.1, ECO:0000313|Proteomes:UP000005263};
RN   [1] {ECO:0000313|EMBL:CCJ07442.1, ECO:0000313|Proteomes:UP000005263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:CCJ07442.1,
RC   ECO:0000313|Proteomes:UP000005263};
RX   PubMed=23045511; DOI=10.1128/JB.01446-12;
RA   Dam B., Dam S., Kube M., Reinhardt R., Liesack W.;
RT   "Complete Genome Sequence of Methylocystis sp. Strain SC2, an Aerobic
RT   Methanotroph with High-Affinity Methane Oxidation Potential.";
RL   J. Bacteriol. 194:6008-6009(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; HE956757; CCJ07442.1; -; Genomic_DNA.
DR   RefSeq; WP_014891471.1; NC_018485.1.
DR   AlphaFoldDB; J7Q8Y6; -.
DR   STRING; 187303.BN69_1991; -.
DR   KEGG; msc:BN69_1991; -.
DR   PATRIC; fig|187303.17.peg.2162; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000005263; 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:CCJ07442.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          641..834
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   995 AA;  111351 MW;  2F57C808768D537F CRC64;
     MARFETNGGA GPAAPVGARS PQNDFLASTS FLQGANAGYL ESLLASYEAD PASVSADWRN
     FFAEMGLRPQ EKVADGPSWA RRDWPQPPNG EWVNAIVGEA PAPVKSPVAP VPAPTPGGED
     VLRATRDSVR ALMMIRAYRM RGHLHANLDP LGLEQRYDHG ELNPQTYGFT DEDYERKIFL
     DGVLGMRYAT LFEMVTILRR TYCGTIGFEF MHISNPEEKA WLQARIEGPK KEIVFTQEGK
     RAILNKLVEA EGFEKFLDVK YTGTKRFGLD GAESIVPALE QIIKRGGALG VKEIVLGMAH
     RGRLNLLSQV MAKPHRALFH EFKGGSFLPD EVEGSGDVKY HLGASSDRVF DDNKVHLSLT
     ANPSHLEIVD PVVLGKVRAK QDQHHCADGD RRSVMPLLIH GDAAFAGQGV VAECFGLSGL
     KGHRTGGSIH FIINNQIGFT TYPRYSRSSP YPSDVAKMVE APILHVNGDD PEAVVFAARV
     AAEFRQQFQK PVVIDMWCYR RFGHNEGDEP GFTQPLMYKK IRAHRTALDI YADRLIAEGV
     TTREDVDRMK EDWRTRLNEE FEAGQSYKPN KADWLDGRWA GKKSGWQLSE NERRGQTGVA
     LETLQHIGAE ITSTPPDFHA HRTIQRFLDN RKAAIEHGGP IDWATAEALA ISSLLYEGYN
     VRLSGQDSER GTFSQRHSVL IDQENEARYL PFNHIAEGQG RYEVVNSMLS EEAVLGFEYG
     YSLAEPDALV LWEAQFGDFA NGAQVVFDQF ISSAERKWLR MSGLVCLLPH GYEGQGPEHS
     SARLERYLQL CAEDNMQVAN CTTPANYFHI LRRQLHRSFR KPLVLMTPKS LLRHKRAVSR
     LGEMGMASSF QRLLLDDAET APNETFILKA DENIRRVILC SGKVYYDLLD EREKRGVDDV
     YLLRVEQLYP FPLKGLVAAL GRFKNADVVW CQEEPKNMGA WSFVDSYLEW VLTQIGGKSK
     RARYVGRAAS ASTATGTMSR HLAQLKLFLE EAFAP
//