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Database: UniProt
Entry: A0A1L8ZS69_9BACI
LinkDB: A0A1L8ZS69_9BACI
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ID   A0A1L8ZS69_9BACI        Unreviewed;       409 AA.
AC   A0A1L8ZS69;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   31-JUL-2019, entry version 13.
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=BLX88_02135 {ECO:0000313|EMBL:OJH20608.1};
OS   Bacillus obstructivus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1914540 {ECO:0000313|EMBL:OJH20608.1, ECO:0000313|Proteomes:UP000182481};
RN   [1] {ECO:0000313|EMBL:OJH20608.1, ECO:0000313|Proteomes:UP000182481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VT-16-70 {ECO:0000313|EMBL:OJH20608.1,
RC   ECO:0000313|Proteomes:UP000182481};
RA   Tetz G., Tetz V.;
RT   "Bacillus obstructivus isolated from the patient with COPD.";
RL   Submitted (NOV-2016) 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:OJH20608.1}.
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DR   EMBL; MPHG01000028; OJH20608.1; -; Genomic_DNA.
DR   RefSeq; WP_071974951.1; NZ_MPHG01000028.1.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000182481; 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; 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   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; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361138};
KW   Complete proteome {ECO:0000313|Proteomes:UP000182481};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182481};
KW   Transferase {ECO:0000256|RuleBase:RU361138,
KW   ECO:0000313|EMBL:OJH20608.1};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        1     76       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      116    153       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       77    177       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    107    129       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    148    170       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   409 AA;  44679 MW;  5B65AB906306D4DA CRC64;
     MAEIKVPELA ESITEGTIAQ WLKQPGDRVE KGEYIVELET DKVNVEVISE EAGVIQELKS
     EEGDTVQVGQ VIAVVSEGGE ASAPANTEKT EAPKQEEKVA AQPQSTPETD KKDRPIASPA
     ARKLAREKGI DLSAVSPVDP MGRVRVQDVN AHTTQPKQEV QASKSAPSAP VSQEDGKPVE
     IVRMSRRRQT IAKRLLEVKQ NTAMLTTFNE IDMTAVMELR KRKKDKFQEE HDGTRLGFMS
     FFTKAVVAAL KKYPAVNSEI QGNELIVKKY YDIGIAVSTD EGLVVPVVRD SDRKNFAEIE
     ADIAGFAKKA RENKLSLGDL QGGTFTITNG GTFGSLFSTP IINGTQVGIL GMHTIQKRPV
     AVGDNIEIRP MMYVALSYDH RVIDGAEAVG FLVTVKKLLE NPEDLLLEA
//
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