ID W9AIN6_9BACI Unreviewed; 432 AA.
AC W9AIN6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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:CDO02792.1};
GN ORFNames=BN988_01268 {ECO:0000313|EMBL:CDO02792.1};
OS Oceanobacillus picturae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=171693 {ECO:0000313|EMBL:CDO02792.1, ECO:0000313|Proteomes:UP000028863};
RN [1] {ECO:0000313|EMBL:CDO02792.1, ECO:0000313|Proteomes:UP000028863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1 {ECO:0000313|EMBL:CDO02792.1,
RC ECO:0000313|Proteomes:UP000028863};
RA Croce O., Lagier J.C., Raoult D.;
RT "Draft genome sequencing of Oceanobacillus picturae strain S1 isolated from
RT human gut.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDO02792.1, ECO:0000313|Proteomes:UP000028863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1 {ECO:0000313|EMBL:CDO02792.1,
RC ECO:0000313|Proteomes:UP000028863};
RA Urmite Genomes U.;
RL Submitted (MAR-2014) 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 -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. Part of the 2-oxoglutarate dehydrogenase (OGDH) complex
CC composed of E1 (2-oxoglutarate dehydrogenase), E2 (dihydrolipoamide
CC succinyltransferase) and E3 (dihydrolipoamide dehydrogenase); the
CC complex contains multiple copies of the three enzymatic components (E1,
CC E2 and E3). {ECO:0000256|ARBA:ARBA00011666}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361138}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDO02792.1}.
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DR EMBL; CCAX010000001; CDO02792.1; -; Genomic_DNA.
DR RefSeq; WP_036574174.1; NZ_QWLU01000010.1.
DR AlphaFoldDB; W9AIN6; -.
DR STRING; 171693.BN988_01268; -.
DR eggNOG; COG0508; Bacteria.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000028863; 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:UP000028863};
KW Transferase {ECO:0000256|RuleBase:RU361138, ECO:0000313|EMBL:CDO02792.1};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU361138}.
FT DOMAIN 1..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 138..175
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 60..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 432 AA; 47966 MW; C25BE7D4A2FDAC35 CRC64;
MKEIKIPELA ESITEGTIAE WLVKKGDKIE KGDPVVELET DKVNVEVNAD YAGVITEILR
EEGDDVEVGD VIAKVDENGE AGGDQEEPKT EEASKEEKQE SSNKESDSQK ESDSEKEEPS
KSEKKDSSSI KSKNGDVIAS PAARKRAREL NIDLSEVSPR DPLGRVRPED VEAAAKGSSK
KEEKKTEKKE ATSEKTEFDK PVERVKMSRR RQTIAKRLVE VQHEAAMLTT FNEVDLTNVM
KLRSDRKEKF IEKHGVKLGF MSFFTKAVVG ALKEFPLLNA EIQGNELVLK KFYDIGIAVS
TDDGLVVPVV RDADRLDFAG VEKEIGNLGK KARDKKLAME DLQGGSFTIT NGGTFGSMLS
TPILNAPQVG ILGMHNIQKR AMVMPDDSIE VRPMMYLALS YDHRIVDGKE AVQFLVRVKE
LLEDPYDLLL EG
//
