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Entry: A0A127MRE1_9PSED
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ID   A0A127MRE1_9PSED        Unreviewed;       411 AA.
AC   A0A127MRE1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex {ECO:0000256|ARBA:ARBA00019511, ECO:0000256|RuleBase:RU361138};
DE            EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945, ECO:0000256|RuleBase:RU361138};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000256|RuleBase:RU361138};
GN   Name=odhB {ECO:0000313|EMBL:WAB90424.1};
GN   ORFNames=A9C11_19020 {ECO:0000313|EMBL:ANI15934.1}, OSS47_20055
GN   {ECO:0000313|EMBL:WAB90424.1};
OS   Pseudomonas citronellolis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=53408 {ECO:0000313|EMBL:WAB90424.1, ECO:0000313|Proteomes:UP001164666};
RN   [1] {ECO:0000313|EMBL:ANI15934.1, ECO:0000313|Proteomes:UP000077748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJTE-3 {ECO:0000313|EMBL:ANI15934.1,
RC   ECO:0000313|Proteomes:UP000077748};
RA   Liang R.;
RT   "Genome Sequence of Pseudomonas citronellolis Strain SJTE-3, an Estrogens
RT   and Persistent Organic Pollutants degradation strain.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:WAB90424.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=G5Li.T10 {ECO:0000313|EMBL:WAB90424.1};
RA   Leung K.M., Lai G.K.K., Leung F.C.C., Griffin S.D.J.;
RT   "Complete genome sequence of Pseudomonas citronellolis G5Li.T10, a toluene-
RT   degrading strain isolated from Hong Kong soil.";
RL   Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E2 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the second step in the conversion of 2-
CC       oxoglutarate to succinyl-CoA and CO(2). {ECO:0000256|ARBA:ARBA00004052,
CC       ECO:0000256|RuleBase:RU361138}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase
CC         complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-
CC         succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC         component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-
CC         COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83120; EC=2.3.1.61;
CC         Evidence={ECO:0000256|ARBA:ARBA00043693,
CC         ECO:0000256|RuleBase:RU361138};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU361138};
CC       Note=Binds 1 lipoyl cofactor covalently.
CC       {ECO:0000256|RuleBase:RU361138};
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC       pathway; glutaryl-CoA from L-lysine: step 6/6.
CC       {ECO:0000256|ARBA:ARBA00005145, ECO:0000256|RuleBase:RU361138}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361138}.
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DR   EMBL; CP015878; ANI15934.1; -; Genomic_DNA.
DR   EMBL; CP113096; WAB90424.1; -; Genomic_DNA.
DR   RefSeq; WP_009619379.1; NZ_PISI01000043.1.
DR   STRING; 53408.A9C11_19020; -.
DR   GeneID; 72995508; -.
DR   KEGG; pcq:PcP3B5_23770; -.
DR   OrthoDB; 9805770at2; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000077748; Chromosome.
DR   Proteomes; UP001164666; Chromosome.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   InterPro; IPR006255; SucB.
DR   NCBIfam; TIGR01347; sucB; 1.
DR   PANTHER; PTHR43416:SF5; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU361138};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361138};
KW   Transferase {ECO:0000256|RuleBase:RU361138, ECO:0000313|EMBL:WAB90424.1};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          111..148
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   411 AA;  43086 MW;  AD0A6FC3567F415A CRC64;
     MAIEIKAPTF PESVADGTVA TWHKKVGEAV KRDELIVDIE TDKVVIEVLA EADGVLAEIV
     KNEGDTVLSN ELLGKLSEGG AAAAAPAPAA AAPAAAPAAA AAPAAAGEDA ILSPAARKLA
     EENGIDPNSI AGTGKGGRVT KEDVVAAVEA KKNAPAAAPA AAKPAAPAAE APVFAAGDRV
     EKRVPMTRLR AKVAERLVEA QSSMAMLTTF NEVNMKPIMD LRNKYKDLFE KKHNGVRLGF
     MSFFVKAATE ALKRFPGVNA SIDGNDIVYH GYQDIGVAVS SDRGLVVPVL RNAEFMSLAE
     IENGIATFGK KAKDGKLSIE DMTGGTFTIS NGGVFGSLLS TPIVNPPQTA ILGMHKIQER
     PMAVNGQVVI LPMMYLALSY DHRMIDGKEA VSFLVAMKDL LEDPARLLLD V
//
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