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Database: UniProt
Entry: A0A0B5E5C1_9RHOB
LinkDB: A0A0B5E5C1_9RHOB
Original site: A0A0B5E5C1_9RHOB 
ID   A0A0B5E5C1_9RHOB        Unreviewed;       508 AA.
AC   A0A0B5E5C1;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   05-JUN-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=P73_3875 {ECO:0000313|EMBL:AJE48590.1};
OS   Celeribacter indicus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Celeribacter.
OX   NCBI_TaxID=1208324 {ECO:0000313|EMBL:AJE48590.1, ECO:0000313|Proteomes:UP000031521};
RN   [1] {ECO:0000313|EMBL:AJE48590.1, ECO:0000313|Proteomes:UP000031521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P73 {ECO:0000313|EMBL:AJE48590.1};
RX   PubMed=25256706; DOI=10.1099/ijs.0.069039-0;
RA   Lai Q., Cao J., Yuan J., Li F., Shao Z.;
RT   "Celeribacter indicus sp. nov., a polycyclic aromatic hydrocarbon-
RT   degrading bacterium from deep-sea sediment and reclassification of
RT   Huaishuia halophila as Celeribacter halophilus comb. nov.";
RL   Int. J. Syst. Evol. Microbiol. 64:4160-4167(2014).
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}.
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DR   EMBL; CP004393; AJE48590.1; -; Genomic_DNA.
DR   RefSeq; WP_043870888.1; NZ_FNNW01000013.1.
DR   EnsemblBacteria; AJE48590; AJE48590; P73_3875.
DR   KEGG; cid:P73_3875; -.
DR   KO; K00658; -.
DR   OrthoDB; 1626282at2; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000031521; Chromosome.
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   ECO:0000313|EMBL:AJE48590.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031521};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031521};
KW   Transferase {ECO:0000256|RuleBase:RU361138,
KW   ECO:0000313|EMBL:AJE48590.1};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      112    187       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      215    252       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION      195    214       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0B5E5C1}.
FT   REGION      255    277       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0B5E5C1}.
SQ   SEQUENCE   508 AA;  53606 MW;  B27A06A1AF8EEAF2 CRC64;
     MSVEVRVPTL GESVTEATVA TWFKKPGETV AVDEMLCELE TDKVTVEVPS PAAGTLGEIV
     AAEGDTVGVD ALLATIAEEG NAGPEETKPR AHAELAEDTP AVTGRATDTA QTLDVMVPTL
     GESVTEATVA TWFKKVGDTV AADEMLCELE TDKVSVEVPA PAAGTLSAIV ANEGDTVAAG
     GKLAELSTGD SVAAAPATAP AAAEPPKPAG GKDVENAPSA TKLMAEKGLD PAQVTGTGKD
     GRIMKEDVLN ALSRPAAQPA PAAAQAPRAP VPADDAAREE RVKMTKLRQT IARRLKESQN
     TAAMLTTYNE VDMTEVMALR NEYKDLFEKK HGVRLGFMSF FTKACCHALK EVPEVNAEID
     GTDVVYKNYV HMGIAAGTPQ GLVVPVIRDA DSMSFAEIEK AVAEKGRRAR DGKLSMAEMQ
     GGTFTISNGG VYGSLMSSPI LNPPQSGILG MHKIQDRPMA INGKVEIRPM MYLALSYDHR
     IVDGKGAVTF LVRVKEALED PRRLLMDL
//
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