GenomeNet

Database: UniProt
Entry: B4W748_9CAUL
LinkDB: B4W748_9CAUL
Original site: B4W748_9CAUL 
ID   B4W748_9CAUL            Unreviewed;       507 AA.
AC   B4W748;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 76.
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=BBAL3_379 {ECO:0000313|EMBL:EDX79222.1};
OS   Brevundimonas sp. BAL3.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=391600 {ECO:0000313|EMBL:EDX79222.1, ECO:0000313|Proteomes:UP000003957};
RN   [1] {ECO:0000313|EMBL:EDX79222.1, ECO:0000313|Proteomes:UP000003957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL3 {ECO:0000313|EMBL:EDX79222.1,
RC   ECO:0000313|Proteomes:UP000003957};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) 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:ARBA00001267,
CC         ECO:0000256|RuleBase:RU361138};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938};
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; DS989898; EDX79222.1; -; Genomic_DNA.
DR   RefSeq; WP_008259347.1; NZ_DS989898.1.
DR   AlphaFoldDB; B4W748; -.
DR   STRING; 391600.BBAL3_379; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_1_5; -.
DR   OrthoDB; 9805770at2; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000003957; 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; 2.
DR   Gene3D; 2.40.50.100; -; 2.
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; 2.
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; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
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:EDX79222.1};
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          108..182
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          217..254
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          197..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   507 AA;  51790 MW;  39D2BD1DD4BFAC88 CRC64;
     MADILTPALG ESVTEATIAK WTKKVGDAVK KDELLVELET DKVSLEVVAP ADGVLGAINA
     AEGDTVVPGT VLGSVTEGGA AAAAAPASAP AKAAKAEAKA APAAAASSID ITVPVMGESV
     AEGSMGKWLK KSGDAVKKDE LLVEIETDKV AVEVSAPADG VLTIAADEGA TVTPGQKIGS
     VSGSGAAASA PAAAAPAPAA APANTGSAQV SGGKNDTLSP AVQRVVAENN LDPKAIAATG
     PKGNITKADA IAAIGQAAPA PTAAAAAPSA PRAVGPREER VKMTRLRQTI ARRLKESQNT
     AAQLTTFNEV DMTNVMALRA QYKEVFEKRH GVKLGFMSFF TKAVVAALHE IPAVNAEIDG
     TDIIYKNHYD IGVAVGTEKG LVVPVLRDAD TLSLAGIEKG IGALGKAARD GALTMDQLQG
     GTFTITNGGT YGSLMSTPIL NAPQSGILGM HNIVQRPMAI NGEVKIRPMM YLALSYDHRI
     VDGKEAVTFL VRIKELLEDP QRALLDL
//
DBGET integrated database retrieval system