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Database: UniProt
Entry: A0A162YX76_9FLAO
LinkDB: A0A162YX76_9FLAO
Original site: A0A162YX76_9FLAO 
ID   A0A162YX76_9FLAO        Unreviewed;       409 AA.
AC   A0A162YX76;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   05-JUN-2019, entry version 15.
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=AWE51_12835 {ECO:0000313|EMBL:KZS39418.1};
OS   Aquimarina aggregata.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aquimarina.
OX   NCBI_TaxID=1642818 {ECO:0000313|EMBL:KZS39418.1, ECO:0000313|Proteomes:UP000076715};
RN   [1] {ECO:0000313|EMBL:KZS39418.1, ECO:0000313|Proteomes:UP000076715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RZW4-3-2 {ECO:0000313|EMBL:KZS39418.1,
RC   ECO:0000313|Proteomes:UP000076715};
RA   Wang Y.;
RT   "The draft genome sequence of Aquimarina sp. RZW4-3-2.";
RL   Submitted (JAN-2016) 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:KZS39418.1}.
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DR   EMBL; LQRT01000035; KZS39418.1; -; Genomic_DNA.
DR   RefSeq; WP_066317663.1; NZ_LQRT01000035.1.
DR   EnsemblBacteria; KZS39418; KZS39418; AWE51_12835.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000076715; 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; 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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361138};
KW   Complete proteome {ECO:0000313|Proteomes:UP000076715};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076715};
KW   Transferase {ECO:0000256|RuleBase:RU361138};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        2     76       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      122    159       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       81    117       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A162YX76}.
FT   REGION      156    176       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A162YX76}.
SQ   SEQUENCE   409 AA;  43539 MW;  69FA860D43898337 CRC64;
     MALEMKVPSP GESITEVEIA QWLVENGDYV EKDQAIAEVD SDKATLELPA EASGVITLMA
     EEGDAVAVGQ VVCLIDTDAA KPAGGGSTPA PAPAAETAKT PEKKEAAPVA APAKTETYAT
     GTASPAAKKV LAEKGIDAAQ VKGTGRDGRI TKADAVDATP SMGTPGLGGR GQSRKKLSML
     RRKVAERLVS VKNETAMLTT FNEVDMQPIF DLRSQHKESF KSKHGVGLGF MSFFTLACVR
     ALKMYPAVNS MIDGDFMVSY DFQDISIAVS GPKGLMVPVI RNAENLSFRG VESEVKRLAI
     RAREGQITVD EMTGGTFTIT NGGVFGSMLS TPIINPPQSA ILGMHNIVER PIVRDGQIVV
     APIMYVALSY DHRIIDGKES VGFLVAVKEA LENPQELLMN NDVMRALEM
//
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