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Database: UniProt
Entry: E2CEG3_9RHOB
LinkDB: E2CEG3_9RHOB
Original site: E2CEG3_9RHOB 
ID   E2CEG3_9RHOB            Unreviewed;       504 AA.
AC   E2CEG3;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   10-APR-2019, entry version 47.
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   Name=sucB {ECO:0000313|EMBL:EFO32817.1};
GN   ORFNames=TRICHSKD4_1435 {ECO:0000313|EMBL:EFO32817.1};
OS   Roseibium sp. TrichSKD4.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Roseibium.
OX   NCBI_TaxID=744980 {ECO:0000313|EMBL:EFO32817.1, ECO:0000313|Proteomes:UP000005735};
RN   [1] {ECO:0000313|EMBL:EFO32817.1, ECO:0000313|Proteomes:UP000005735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TrichSKD4 {ECO:0000313|EMBL:EFO32817.1,
RC   ECO:0000313|Proteomes:UP000005735};
RA   Mann E., Barbeau K., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (MAR-2010) 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}.
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DR   EMBL; GL476310; EFO32817.1; -; Genomic_DNA.
DR   RefSeq; WP_009466616.1; NZ_GL476310.1.
DR   STRING; 744980.TRICHSKD4_1435; -.
DR   EnsemblBacteria; EFO32817; EFO32817; TRICHSKD4_1435.
DR   eggNOG; ENOG4105C7S; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   OrthoDB; 1626282at2; -.
DR   BioCyc; RSP744980:G1GND-1271-MONOMER; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000005735; 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; 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; PS00189; LIPOYL; 2.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361138,
KW   ECO:0000313|EMBL:EFO32817.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005735};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005735};
KW   Transferase {ECO:0000256|RuleBase:RU361138,
KW   ECO:0000313|EMBL:EFO32817.1};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      106    181       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      211    248       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   504 AA;  51829 MW;  E400AB8B0AC85992 CRC64;
     MATEIRVPTL GESVSEATIA QWFKKPGDAI TADEPIVELE TDKVTVEVPA PASGTLESIV
     VNEGDTVEVG ALLGQIADGA GAATAPAAAA AAEAPAAPAA AAGGNVVDVV TPSAGESVTE
     AEVGEWSVKV GDVVKADDTL VELETDKAAQ EVPAPVAGTV VKIAAETGAT VEPGTLLCQI
     DTSGAGASAA AAAVSAPAAA PAPAASGTSM PPAPSAAKMI AEKNIAADQV VGSGKRGQVL
     KGDVIAAASA GINAPAPAAT AVPRGPVAAD DEVREERVRM TKLRQTIARR LKDAQNSAAM
     LTTYNEVDMG PVMELRKQYK DLFEKKHGVK LGFMGFFTKA VCHALKEIPA VNAEIDGTDM
     IYKNFCHIGV AVGTDKGLVV PVVRDADQMS IAEVEQEIGN LGRKARDGKL GMADMTGGTF
     TISNGGVYGS LMSSPILNAP QSGILGMHKI QERPMAVNGQ VVIRPMMYLA LSYDHRIVDG
     KEAVTFLVRV KESLEDPQRL VLDL
//
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