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Database: UniProt
Entry: A0A1M6DTP8_9FLAO
LinkDB: A0A1M6DTP8_9FLAO
Original site: A0A1M6DTP8_9FLAO 
ID   A0A1M6DTP8_9FLAO        Unreviewed;       403 AA.
AC   A0A1M6DTP8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   05-JUN-2019, entry version 11.
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=SAMN05216261_1741 {ECO:0000313|EMBL:SHI76572.1};
OS   Arenitalea lutea.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1178825 {ECO:0000313|EMBL:SHI76572.1, ECO:0000313|Proteomes:UP000184396};
RN   [1] {ECO:0000313|EMBL:SHI76572.1, ECO:0000313|Proteomes:UP000184396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12213 {ECO:0000313|EMBL:SHI76572.1,
RC   ECO:0000313|Proteomes:UP000184396};
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; FQYK01000003; SHI76572.1; -; Genomic_DNA.
DR   RefSeq; WP_019386719.1; NZ_FQYK01000003.1.
DR   STRING; 1178825.ALIH01000003_gene2028; -.
DR   OrthoDB; 1626282at2; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000184396; 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:UP000184396};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184396};
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      116    153       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       80    114       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1M6DTP8}.
FT   REGION      152    172       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1M6DTP8}.
FT   COMPBIAS     85    103       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1M6DTP8}.
SQ   SEQUENCE   403 AA;  43265 MW;  C58CDF6BA191E6E4 CRC64;
     MILEMKVPSP GESITEVEIA TWLVEDGDYV EKDQAIAEVD SDKATLELPA EANGIITLKA
     EEGDAVAVGA VVCLIDTSAE KPEGSDAPQT EEKKSEAPKA ETPKAPAEAK TYATGTASPA
     AKKILAEKGM DVSAISGTGK DGRITKDDAV KAVPSMGTPT GGNRGTSRTK MSMLRRKVAE
     RLVEAKNTTA MLTTFNEVDM SPIFALRSEY KETFKTKHGV SLGFMSFFTL AIVRALKMYP
     AVNSMIDGKE MLSYDFCDIS IAVSGPKGLM VPVIRNAENL SFRGVESEVK RLALRARDGQ
     ITVDEMTGGT FTITNGGVFG SMLSTPIINP PQSGILGMHN IVERPVAIDG KVEIRPIMYV
     ALSYDHRIID GKESVGFLVA VKEALENPIE LLMDNDVKKA LEL
//
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