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Database: UniProt
Entry: A0A1M5D9Z9_9FLAO
LinkDB: A0A1M5D9Z9_9FLAO
Original site: A0A1M5D9Z9_9FLAO 
ID   A0A1M5D9Z9_9FLAO        Unreviewed;       402 AA.
AC   A0A1M5D9Z9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   05-JUN-2019, entry version 10.
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=SAMN05444344_0909 {ECO:0000313|EMBL:SHF63685.1};
OS   Tenacibaculum mesophilum.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=104268 {ECO:0000313|EMBL:SHF63685.1, ECO:0000313|Proteomes:UP000183998};
RN   [1] {ECO:0000313|EMBL:SHF63685.1, ECO:0000313|Proteomes:UP000183998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13764 {ECO:0000313|EMBL:SHF63685.1,
RC   ECO:0000313|Proteomes:UP000183998};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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}.
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DR   EMBL; FQVV01000001; SHF63685.1; -; Genomic_DNA.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000183998; 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:UP000183998};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183998};
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      115    152       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       83    118       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1M5D9Z9}.
FT   COMPBIAS     90    106       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1M5D9Z9}.
SQ   SEQUENCE   402 AA;  43334 MW;  527CA4C8C1CE0F08 CRC64;
     MVLEMKVPSP GESITEVEIA TWLVEDGDYV EKDQPIAEVD SDKATLELPA EESGIITLKA
     EEGDAVAVGA VVCHIDMDAA KPDEAGAPKA AAPKTEEKKE APKAEPAKET YATGTASPAA
     KKVLAEKGMN PSDVKGTGKD GRVTKEDAVK AVPSMGTPGM GSRGTERKKL SMLRRKVAQR
     LVSVKNETAM LTTFNEVNMQ PIFDLRNEYK EAFKAKHGVG LGFMSFFTLA VVRALKMYPD
     VNSMIDGDYK VSHDFQDISI AVSGPKGLMV PVIRNAENLT FRGVESEVKR LALRARDGQI
     TVDEMTGGTF TITNGGVFGS MLSTPIINPP QSGILGMHNI VNRPMAVNGE VVIQPIMYVA
     LSYDHRIIDG RESVGFLVAV KEALENPVEL LMNNNPTKAL EM
//
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