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Database: UniProt
Entry: K6E4L3_BACAZ
LinkDB: K6E4L3_BACAZ
Original site: K6E4L3_BACAZ 
ID   K6E4L3_BACAZ            Unreviewed;       411 AA.
AC   K6E4L3;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   10-APR-2019, entry version 35.
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=BAZO_05485 {ECO:0000313|EMBL:EKN68186.1};
OS   Bacillus azotoformans LMG 9581.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1131731 {ECO:0000313|EMBL:EKN68186.1, ECO:0000313|Proteomes:UP000006315};
RN   [1] {ECO:0000313|EMBL:EKN68186.1, ECO:0000313|Proteomes:UP000006315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 9581 {ECO:0000313|EMBL:EKN68186.1,
RC   ECO:0000313|Proteomes:UP000006315};
RX   PubMed=23087684;
RA   Heylen K., Keltjens J.;
RT   "Redundancy and modularity in membrane-associated dissimilatory
RT   nitrate reduction in Bacillus.";
RL   Front. Microbiol. 3:371-371(2012).
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:EKN68186.1}.
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DR   EMBL; AJLR01000041; EKN68186.1; -; Genomic_DNA.
DR   RefSeq; WP_003330308.1; NZ_AJLR01000041.1.
DR   EnsemblBacteria; EKN68186; EKN68186; BAZO_05485.
DR   PATRIC; fig|1131731.3.peg.1145; -.
DR   OrthoDB; 1626282at2; -.
DR   BioCyc; GCF_000307855:G1EGP-1098-MONOMER; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000006315; 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   ECO:0000313|EMBL:EKN68186.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006315};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006315};
KW   Transferase {ECO:0000256|RuleBase:RU361138,
KW   ECO:0000313|EMBL:EKN68186.1};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        1     76       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      107    144       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   411 AA;  46247 MW;  2A0FBAD35429C00C CRC64;
     MMEIKVPELA ESINEGTIVE WLKQEGDYVQ NGEPIAELET DKINVEINSD FSGIIKQFLF
     MPGDTVQVGQ VIAILDENEN HFGNVPEPEL KPESLILEKE KPNNNLVASP AARKRARELG
     VSLDEIPYKD PLGRIRVEDV EDYKKSHRDL TNNEPNHQPA NTVTKNQSNQ LKVDEKDQQI
     ERVKMSRRRQ TIANRLLEAQ HNAAMLTTFN EVDMTAIMDV RNRRKESFNK KHGVKLGFMS
     FFTKAVIGAL KEFPFLNAEI QGDEILIKKF YDIGVAVSTD DGLVVPVVRD ADRLSFAGIE
     KEIGVLSEKA RNKSLGLKDL QGGTFTITNG GIFGSLYSTP ILNAPQVGIL GMHKIQRRPV
     VIDDEDTIEV RPMMYIALSY DHRIIDGKDA VQFLVKIKEL LESPEDLLLE G
//
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