ID   S6GLP0_9GAMM            Unreviewed;       407 AA.
AC   S6GLP0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   ORFNames=OFPII_01020 {ECO:0000313|EMBL:EPJ49437.1};
OS   Osedax symbiont Rs1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae.
OX   NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ49437.1, ECO:0000313|Proteomes:UP000014822};
RN   [1] {ECO:0000313|EMBL:EPJ49437.1, ECO:0000313|Proteomes:UP000014822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822};
RA   Yi H., Goffredi S.;
RT   "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT   Osedax worms: functional variation and environmental selection.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938,
CC         ECO:0000256|RuleBase:RU003423};
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {ECO:0000256|ARBA:ARBA00011484}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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:EPJ49437.1}.
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DR   EMBL; ASZJ01000007; EPJ49437.1; -; Genomic_DNA.
DR   AlphaFoldDB; S6GLP0; -.
DR   PATRIC; fig|1330036.3.peg.95; -.
DR   Proteomes; UP000014822; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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   PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 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|RuleBase:RU003423,
KW   ECO:0000313|EMBL:EPJ49437.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014822};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EPJ49437.1}.
FT   DOMAIN          3..80
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          119..156
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   407 AA;  43908 MW;  ECCECC0EEEFBCCC9 CRC64;
     MSQFSFKLPD LGEGIVASEI VEWHVKVGDT VSEDQHIVDV MTDKAVVEVT APVSGVVAKL
     ACEAGIEIPV GSELILFTLE ENSQSAAQDE RPPTPVAAPQ AVSCLSTNDP VQVLSKTVLS
     SPSVRRHARE GNIDLSLVSG TGTAGRINNS DLQDFIDNGG QQVSKVAATC STIDADFASK
     DIKISGLRRV IAKKMLQATH NIPHYSYIEE IDLTALDTLR EHLNKHRKDD QQKLTLLPFI
     MQTLVKVIRD FPHCNAHYNA ETEILTQYSA VDVGIATMTE QGLLVPVIKN TQQLDIWQSA
     AQLSKITAIT RSGGAKAQQL TGSTITITSL GAIGGIATTP IINAPETTII GINKMQLRPV
     VIDGKIVIRK MMNLSSSFDH RIVDGYDGAL FIQALKTLLE NPGAIFV
//