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Database: UniProt
Entry: A0A0Q7SNG7_9BACL
LinkDB: A0A0Q7SNG7_9BACL
Original site: A0A0Q7SNG7_9BACL 
ID   A0A0Q7SNG7_9BACL        Unreviewed;       424 AA.
AC   A0A0Q7SNG7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   05-JUN-2019, entry version 22.
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=ASD24_09330 {ECO:0000313|EMBL:KQY83993.1};
OS   Paenibacillus sp. Root52.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1736552 {ECO:0000313|EMBL:KQY83993.1, ECO:0000313|Proteomes:UP000051734};
RN   [1] {ECO:0000313|EMBL:KQY83993.1, ECO:0000313|Proteomes:UP000051734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root52 {ECO:0000313|EMBL:KQY83993.1,
RC   ECO:0000313|Proteomes:UP000051734};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY83993.1, ECO:0000313|Proteomes:UP000051734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root52 {ECO:0000313|EMBL:KQY83993.1,
RC   ECO:0000313|Proteomes:UP000051734};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQY83993.1}.
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DR   EMBL; LMFO01000023; KQY83993.1; -; Genomic_DNA.
DR   RefSeq; WP_056698729.1; NZ_LMFO01000023.1.
DR   EnsemblBacteria; KQY83993; KQY83993; ASD24_09330.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000051734; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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:0009306; P:protein secretion; IEA:InterPro.
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:UP000051734};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138, ECO:0000256|SAAS:SAAS00065550};
KW   Transferase {ECO:0000256|RuleBase:RU361138,
KW   ECO:0000313|EMBL:KQY83993.1};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        1     76       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      126    163       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       73    133       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0Q7SNG7}.
FT   REGION      160    199       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0Q7SNG7}.
FT   COMPBIAS     77    101       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0Q7SNG7}.
FT   COMPBIAS    178    194       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0Q7SNG7}.
SQ   SEQUENCE   424 AA;  45297 MW;  A058B718F0668F37 CRC64;
     MSEIKVPAMG ESITEGTVSK WLVKEGDTVN QGDVLLELET DKVNIEISAE ESGVLEKIIR
     QEGDTVEIGE TIGTLSAGAG GGSSSAASEP AASEQKQATT PAPEAPTPPP APVAAGSESS
     DNGNKTASPS ARKLARERGI ELDQVHGKDP IGRVYQDDVK AHSTQATAPA APSANKAPAA
     SSAPTGGSTY TKPVERQRMS RRRATIAKRL VEAQQTAAML TTFNEVDMTA IMDVRKRRKD
     KFKEKHEINL GFMSFFTKAV VGALKKFPTI NAEIDGEDVV LKKYYDIGIA VSAKEGLVVP
     VVRDADRLGF AEIERSIADL ASKARSNTLA LSDLQGGTFT ITNGGTFGSL LSTPILNTPQ
     VGILGMHKIQ LRPVAIDAER MENRPMMYIA LSYDHRIIDG SEAVRFLVTV KELLEDPESL
     LIEG
//
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