GenomeNet

Database: UniProt
Entry: A0A0T5NWU6_9RHOB
LinkDB: A0A0T5NWU6_9RHOB
Original site: A0A0T5NWU6_9RHOB 
ID   A0A0T5NWU6_9RHOB        Unreviewed;       531 AA.
AC   A0A0T5NWU6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   31-JUL-2019, entry version 18.
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=XM53_07365 {ECO:0000313|EMBL:KRS13396.1};
OS   Roseovarius atlanticus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Roseovarius.
OX   NCBI_TaxID=1641875 {ECO:0000313|EMBL:KRS13396.1, ECO:0000313|Proteomes:UP000051295};
RN   [1] {ECO:0000313|EMBL:KRS13396.1, ECO:0000313|Proteomes:UP000051295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R12B {ECO:0000313|EMBL:KRS13396.1,
RC   ECO:0000313|Proteomes:UP000051295};
RA   Li G., Lai Q., Shao Z., Yan P.;
RT   "The draft genome sequence of Roseovarius sp.R12b.";
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   -!- 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:KRS13396.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; LAXJ01000006; KRS13396.1; -; Genomic_DNA.
DR   RefSeq; WP_057791841.1; NZ_LAXJ01000006.1.
DR   EnsemblBacteria; KRS13396; KRS13396; XM53_07365.
DR   PATRIC; fig|1641875.4.peg.3859; -.
DR   OrthoDB; 1626282at2; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000051295; 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; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   TIGRFAMs; TIGR01347; sucB; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361138};
KW   Complete proteome {ECO:0000313|Proteomes:UP000051295};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051295};
KW   Transferase {ECO:0000256|RuleBase:RU361138};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      117    192       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      235    272       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       76    122       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      196    261       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      274    304       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     84    103       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   531 AA;  55857 MW;  154D36E3EBF6372D CRC64;
     MTTEVRVPTL GESVTEATVA TWFKKAGDTV EADEMLCELE TDKVTVEVPS PAAGTLAEIV
     AQEGETVGVD ALLATLSEGD SGSDSAPKKA EKKEEKKTEP APAKSGGDSD GSGGGGNIDV
     MVPTLGESVS EATVSTWFKK VGDNVSQDEM LCELETDKVS VEVPSPAAGT LTEILANEGD
     TVQANGKLAV LSGAADGAVE PAERPDSNAI PAQGDEPATA NGGQYTAPLP GRDIEDAPSA
     KKAMAEKGLS SDQVQGSGRD GRVMKEDVAK AAAAATSAAP ATSSAPAQAP RAPVSAEDAS
     REERVKMTRL RQTIARRLKD SQNTAAMLTT YNEVDMTEVM ALRNQYKDEF QKKHGVKLGF
     MSFFTKACCH ALKEVPEVNA EIDGTDIVYK NFVHMGIATG TPTGLVVPVI RDADALGFAD
     IEKAIAEKGA RARDGKLSMA EMQGGTFTIS NGGVYGSLMS SPILNPPQSG ILGMHKIQQR
     PMVVNGEIKA RPMMYLALSY DHRIVDGKGA VTFLVRVKDA LEDPRRLLMD L
//
DBGET integrated database retrieval system