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Database: UniProt
Entry: F7NY10_9GAMM
LinkDB: F7NY10_9GAMM
Original site: F7NY10_9GAMM 
ID   F7NY10_9GAMM            Unreviewed;       395 AA.
AC   F7NY10;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex {ECO:0000256|ARBA:ARBA00019511, ECO:0000256|RuleBase:RU361138};
DE            EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945, ECO:0000256|RuleBase:RU361138};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000256|RuleBase:RU361138};
GN   ORFNames=Rhein_2586 {ECO:0000313|EMBL:EGM77304.1};
OS   Rheinheimera sp. A13L.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Rheinheimera.
OX   NCBI_TaxID=506534 {ECO:0000313|EMBL:EGM77304.1, ECO:0000313|Proteomes:UP000004282};
RN   [1] {ECO:0000313|EMBL:EGM77304.1, ECO:0000313|Proteomes:UP000004282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A13L {ECO:0000313|EMBL:EGM77304.1,
RC   ECO:0000313|Proteomes:UP000004282};
RX   PubMed=21742876; DOI=10.1128/JB.05636-11;
RA   Gupta H.K., Gupta R.D., Singh A., Chauhan N.S., Sharma R.;
RT   "Genome Sequence of Rheinheimera sp. Strain A13L, Isolated from Pangong
RT   Lake, India.";
RL   J. Bacteriol. 193:5873-5874(2011).
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). {ECO:0000256|ARBA:ARBA00004052,
CC       ECO:0000256|RuleBase:RU361138}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase
CC         complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-
CC         succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC         component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-
CC         COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83120; EC=2.3.1.61;
CC         Evidence={ECO:0000256|ARBA:ARBA00001267,
CC         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 saccharopine
CC       pathway; glutaryl-CoA from L-lysine: step 6/6.
CC       {ECO:0000256|ARBA:ARBA00005145, ECO:0000256|RuleBase:RU361138}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361138}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGM77304.1}.
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DR   EMBL; AFHI01000023; EGM77304.1; -; Genomic_DNA.
DR   RefSeq; WP_008899437.1; NZ_AFHI01000023.1.
DR   AlphaFoldDB; F7NY10; -.
DR   STRING; 506534.Rhein_2586; -.
DR   eggNOG; COG0508; Bacteria.
DR   OrthoDB; 9805770at2; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000004282; 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   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 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   NCBIfam; TIGR01347; sucB; 1.
DR   PANTHER; PTHR43416:SF5; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 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|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU361138};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361138};
KW   Transferase {ECO:0000256|RuleBase:RU361138, ECO:0000313|EMBL:EGM77304.1};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN          1..75
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          105..142
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   395 AA;  42397 MW;  0C6FFF00289C2BAD CRC64;
     MEIKVPVLPE SVADATIATW HVKTGEAVSR DQVLVDIETD KVVLEVVAQA DGVMGEIVHA
     EGATVLAEQV IGHMNAGAAA PAAAPAAKAD AAPAAAAPAA ESDDVLTPSV RRLIAEKGLD
     AAKIQGSGKN GRVTKEDVEK FLAGAPAAPA KAAVAAPAPV QGDRSQKRVP MTRLRKTIAN
     RLLEAKNSTA MLTTFNEVNM KPIMDLRKQY QDVFEKRHGI RLGFMSFYVK AVTEALKRFP
     EVNAAIDGDD IVYHNYFDVS IAVSTPRGLV TPVLRDCDKM NLAEIEKAIK DLALKGRDGK
     LSMDDLTGGN FTITNGGVFG SLMSTPIINP PQSAILGMHK IQDRVMVVDG KMEILPMMYL
     ALSYDHRIID GKESVGFLVT IKELLEDPTR ILLDI
//
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