ID Q9R8R0_PSEPU Unreviewed; 407 AA.
AC Q9R8R0;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 108.
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=kgdB {ECO:0000313|EMBL:AAC23517.1};
GN Synonyms=sucB {ECO:0000313|EMBL:BBU45956.1};
GN ORFNames=PPTS312_38710 {ECO:0000313|EMBL:BBU45956.1};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303 {ECO:0000313|EMBL:AAC23517.1};
RN [1] {ECO:0000313|EMBL:AAC23517.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PpG2 {ECO:0000313|EMBL:AAC23517.1};
RA Madhusudhan K.T., Clifton S., Roe B.A.;
RT "Nucleotide sequence of genes encoding alpha-ketoglutarate dehydrogenase
RT and dihydrolipoamide succinyltransferase components of Pseudomonas putida
RT PpG2.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BBU45956.1, ECO:0000313|Proteomes:UP000464661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TS312 {ECO:0000313|EMBL:BBU45956.1,
RC ECO:0000313|Proteomes:UP000464661};
RA Hosoe A., Suenaga T., Sugi T., Izumi T., Nagai N., Terada A.;
RT "Complete Genome Sequence of Pseudomonas putida Strain TS312, Harboring the
RT HdtS type N-acyl-homoserine Lactone Synthase, Isolated from a Paper Mill.";
RL Submitted (JAN-2020) 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; AF068740; AAC23517.1; -; Genomic_DNA.
DR EMBL; AP022324; BBU45956.1; -; Genomic_DNA.
DR PIR; B39406; B39406.
DR AlphaFoldDB; Q9R8R0; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000464661; 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:AAC23517.1};
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 108..145
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 407 AA; 42350 MW; 1493AB07FE17B177 CRC64;
MAIEIKAPTF PESVADGTVA TWHKQPGEAV KRDELIVDIE TDKVVLEVLA TADGVLGAIV
KGEGDTVLSD EVLGSIVEGG AAAAAPAAAP AAAAPAAAAA DAGEDDPIAA PAARKLAEEN
GIDLAAVTGT GKGGRITKED VVAAVANKKS APAAAPAAKP AAAAAAPVVV AAGDRTEKRV
PMTRLRAKIA ERLVEAQSSM AMLTTFNEVD MTEVMALRSK YKDLFEKTHN GVRLGFMSFF
VKAATEALKR FPAVNASIDG NDIVYHGYAD VGVAVSSDRG LVVPVLRNAE SMSLAEIENG
IATFGKKARD GKLAIEEMTG GTFTITNGGT FGSMMSTPIV NPPQAAILGM HNIIQRPMAI
NGQVVIRPMM YLALSYDHRL IDGKEAVTFL VTIKNLLEDP SRLLLDI
//
