ID A0A0B3BQ03_9PSED Unreviewed; 403 AA.
AC A0A0B3BQ03; A0A0B2D8J4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 ORFNames=PT85_03225 {ECO:0000313|EMBL:KHO66583.1}, SAMN05421672_10868
GN {ECO:0000313|EMBL:SIQ61998.1};
OS Pseudomonas flexibilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=706570 {ECO:0000313|EMBL:KHO66583.1, ECO:0000313|Proteomes:UP000030980};
RN [1] {ECO:0000313|EMBL:KHO66583.1, ECO:0000313|Proteomes:UP000030980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14085 {ECO:0000313|EMBL:KHO66583.1,
RC ECO:0000313|Proteomes:UP000030980};
RA Shin S.-K., Yi H.;
RT "Genome sequence of Pseudomonas tuomuerensis JCM 14085.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SIQ61998.1, ECO:0000313|Proteomes:UP000186079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29606 {ECO:0000313|EMBL:SIQ61998.1,
RC ECO:0000313|Proteomes:UP000186079};
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: 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JTAK01000001; KHO66583.1; -; Genomic_DNA.
DR EMBL; FTMC01000008; SIQ61998.1; -; Genomic_DNA.
DR RefSeq; WP_027590088.1; NZ_JTAK01000001.1.
DR AlphaFoldDB; A0A0B3BQ03; -.
DR STRING; 706570.PT85_03225; -.
DR PATRIC; fig|706570.3.peg.2287; -.
DR OrthoDB; 9805770at2; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000030980; Unassembled WGS sequence.
DR Proteomes; UP000186079; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000030980};
KW Transferase {ECO:0000256|RuleBase:RU361138, ECO:0000313|EMBL:KHO66583.1};
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 107..144
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 403 AA; 42214 MW; 5FB3B6935D1A9E80 CRC64;
MAIEIKAPAF PESVADGTVA TWHKKPGEAV KRDELIVDIE TDKVVMEVLA EADGVVGEII
KGEGETVLSG EVLGTLNAGA VAAAPAPAAA AAPAAAAAPA AAAEDKILSP AARKIADEAG
VDRNSIEGTG KGGRVTKEDA VAAASGKPAA APAAKTAAPA ADAPVFAAGD RVEKRVPMTR
LRAKVAQRLV EAQSSMAMLT TYNEVNMKPI MDLRAKYKDL FEKKHNGVRL GFMSFFVKAA
VEALKRQPVV NASIDGNDIV YHGYQDIGVA VSSDRGLVVP VLRNAEFMSL AEIEGGIAAY
GRKAKEGKLT IEEMTGGTFT ISNGGVFGSL LSSPIVNPPQ SAILGMHKIQ ERPMAVNGQV
VILPMMYLAL SYDHRLLDGK EAVTFLVTLK DLLEDPARLL LDI
//
