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Database: UniProt
Entry: A0A086A6J8_9FLAO
LinkDB: A0A086A6J8_9FLAO
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ID   A0A086A6J8_9FLAO        Unreviewed;       417 AA.
AC   A0A086A6J8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   31-JUL-2019, entry version 27.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex {ECO:0000256|RuleBase:RU361138};
DE            EC=2.3.1.61 {ECO:0000256|RuleBase:RU361138};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000256|RuleBase:RU361138};
GN   ORFNames=IW15_12195 {ECO:0000313|EMBL:KFF12312.1};
OS   Chryseobacterium soli.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Chryseobacterium.
OX   NCBI_TaxID=445961 {ECO:0000313|EMBL:KFF12312.1, ECO:0000313|Proteomes:UP000028705};
RN   [1] {ECO:0000313|EMBL:KFF12312.1, ECO:0000313|Proteomes:UP000028705}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19298 {ECO:0000313|EMBL:KFF12312.1,
RC   ECO:0000313|Proteomes:UP000028705};
RA   Stropko S.J., Pipes S.E., Newman J.;
RT   "Genome of Chryseobacterium soli DSM 19298.";
RL   Submitted (JUL-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).
CC       {ECO:0000256|RuleBase:RU361138}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate
CC         dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-
CC         (S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate
CC         dehydrogenase complex component E2] + CoA; Xref=Rhea:RHEA:15213,
CC         Rhea:RHEA-COMP:10581, Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:83100, ChEBI:CHEBI:83120;
CC         EC=2.3.1.61; Evidence={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
CC       saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
CC       {ECO:0000256|RuleBase:RU361138}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361138}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KFF12312.1}.
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DR   EMBL; JPRH01000004; KFF12312.1; -; Genomic_DNA.
DR   RefSeq; WP_034711461.1; NZ_JPRH01000004.1.
DR   STRING; 445961.IW15_12195; -.
DR   EnsemblBacteria; KFF12312; KFF12312; IW15_12195.
DR   OrthoDB; 1626282at2; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000028705; 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   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 1.
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   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR01347; sucB; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361138};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028705};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138};
KW   Transferase {ECO:0000256|RuleBase:RU361138};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        3     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      126    163       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       85    123       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   417 AA;  44404 MW;  4D4F975CDC090871 CRC64;
     MSILEMKVPS PGESITEVEI ATWLVKDGDY VEKDQPIAEV DSDKATLELP AEESGIITLK
     AEEGDVVQVG QVVCLIDRDA AKPEGAAAPA AEAPKKEEAP KAAEPVKAEA PKPAVQAAAQ
     TYATGAPSPA AKKILDEKGV DAGQVSGSGR DGRITKTDAE LAAVPAMGGS SLSATGSRAS
     TTTKLSVLRR KIASRLVSVK NETAMLTTFN EVDMSEIFRL RKLYKEEFAQ KHGVGIGFMS
     FFTKAVTRAL KMYPDVNASI DGDFKINYDF CDISIAVSGP KGLMVPVLRN AENMSFKGIE
     ANIKDLATKV RDGKISVDEM TGGTFTITNG GTFGSMLSTP IINPPQSAIL GMHNIIQRPV
     AVDGQVVIRP MMYVAMSYDH RIIDGKESVG FLVAVKEGID NPVEILMGGD ERRGLEL
//
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