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Database: UniProt
Entry: A0A0G9MYN2_9SPHN
LinkDB: A0A0G9MYN2_9SPHN
Original site: A0A0G9MYN2_9SPHN 
ID   A0A0G9MYN2_9SPHN        Unreviewed;       425 AA.
AC   A0A0G9MYN2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   31-JUL-2019, entry version 23.
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=AAW00_05680 {ECO:0000313|EMBL:KLE35851.1};
OS   Erythrobacter luteus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=1581420 {ECO:0000313|EMBL:KLE35851.1, ECO:0000313|Proteomes:UP000053464};
RN   [1] {ECO:0000313|EMBL:KLE35851.1, ECO:0000313|Proteomes:UP000053464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA37 {ECO:0000313|EMBL:KLE35851.1,
RC   ECO:0000313|Proteomes:UP000053464};
RA   Zhuang L., Liu Y., Shao Z.;
RT   "The draft genome sequence of Erythrobacter luteus KA37.";
RL   Submitted (APR-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:KLE35851.1}.
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DR   EMBL; LBHB01000001; KLE35851.1; -; Genomic_DNA.
DR   RefSeq; WP_047003255.1; NZ_LBHB01000001.1.
DR   EnsemblBacteria; KLE35851; KLE35851; AAW00_05680.
DR   PATRIC; fig|1581420.6.peg.1145; -.
DR   OrthoDB; 1626282at2; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000053464; 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:UP000053464};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053464};
KW   Transferase {ECO:0000256|RuleBase:RU361138,
KW   ECO:0000313|EMBL:KLE35851.1};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      128    165       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       82    103       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      167    199       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   425 AA;  44439 MW;  98A7C4C0C57932FF CRC64;
     MSTEVKVPTL GESVTEATVG EWLKQPGDAV AVDEPIASLE TDKVAVEVPS PVAGRLESHA
     VEVGATVEVG AVIALVTAGD TAPAEKAPAA QPKADKALAD KQSSDEIAAL PDDKAAASGA
     PAGDGSVTMS PAVRRAVIEH GVDPTSIKGT GKDGRLTKED VIAAAEAKKA APSDASAPAA
     PAPAPVPAAA KGERREERVK MTRMRQTIAK RLKGAQDNAA LLTTFNDCDM TAVIEAREAY
     KDLFAKKHGI KLGFMSFFAK AACLALKDVP AVNAYIDGDE IVYHDYVDIS VAVSAPNGLV
     VPVVRSADAM SFAEIELAIA DFGKRAKEGA LTMDDMAGGT FTISNGGVFG SLMSTPIINP
     PQSAVLGLHR IEDRPVARNG EVVIRPMMYL ALSYDHRIID GREAVTALKI MKEAIEDPMR
     LLIDL
//
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