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Database: UniProt
Entry: T0LEZ8_9BACT
LinkDB: T0LEZ8_9BACT
Original site: T0LEZ8_9BACT 
ID   T0LEZ8_9BACT            Unreviewed;       423 AA.
AC   T0LEZ8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   31-JUL-2019, entry version 34.
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=RBG1_1C00001G0523 {ECO:0000313|EMBL:EQB62944.1};
OS   candidate division Zixibacteria bacterium RBG-1.
OC   Bacteria.
OX   NCBI_TaxID=1379698 {ECO:0000313|EMBL:EQB62944.1, ECO:0000313|Proteomes:UP000015604};
RN   [1] {ECO:0000313|EMBL:EQB62944.1, ECO:0000313|Proteomes:UP000015604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Castelle C.J., Hug L.A., Wrighton K.C., Thomas B.C., Williams K.H.,
RA   Wu D., Tringe S.G., Singer S.W., Eisen J.A., Banfield J.F.;
RT   "Extraordinary phylogenetic diversity and metabolic versatility in
RT   aquifer sediment.";
RL   Submitted (JUL-2013) 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:EQB62944.1}.
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DR   EMBL; AUYT01000001; EQB62944.1; -; Genomic_DNA.
DR   STRING; 1379698.RBG1_1C00001G0523; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000015604; 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:UP000015604};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:EQB62944.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015604};
KW   Transferase {ECO:0000256|RuleBase:RU361138,
KW   ECO:0000313|EMBL:EQB62944.1};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      127    164       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       88    124       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   423 AA;  46602 MW;  E990B9DDEAC4E6E1 CRC64;
     MPIPIVVPQL GESVVEGTVG KWLKKEGEKV AKDEPIVEIM TDKINVEIPS PKAGVLAKIL
     VPENTVVPIG QEIGILAEAG ESISNISASA SPAPAKTEVK PQPTQPKPEV RASGSVAVED
     AKTDQARLSP AVRRLVKENN IDISKINGTG SGGRITREDI LAYLEKGGTP ATTKAPAIQP
     KVVAAPTTAG PLEEVLPLTF VRKKISEHMS LSRRTVAHCT TWDEADMKKL VEIREKLKEP
     FQKKHNLKLT YMPFIMKATV FALKEYPHMN ASMTEENMIV KKYYHLGMAV GREVGLIVVV
     VRDCDKKSIL EITREINELG DKARADKLSL NDIQGSTFTI TNAGMFGALA STPIINYPEV
     GILGIHMIQK RAVVVDDQIV IRPMMTMCLS FDHRLIDGHY AVQFLQRVKY YLESPEEWLL
     NIM
//
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