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Database: UniProt
Entry: A0A066RQH1_9GAMM
LinkDB: A0A066RQH1_9GAMM
Original site: A0A066RQH1_9GAMM 
ID   A0A066RQH1_9GAMM        Unreviewed;       386 AA.
AC   A0A066RQH1;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=EA58_20005 {ECO:0000313|EMBL:KDM89942.1};
OS   Photobacterium galatheae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=1654360 {ECO:0000313|EMBL:KDM89942.1, ECO:0000313|Proteomes:UP000027192};
RN   [1] {ECO:0000313|EMBL:KDM89942.1, ECO:0000313|Proteomes:UP000027192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2753 {ECO:0000313|EMBL:KDM89942.1,
RC   ECO:0000313|Proteomes:UP000027192};
RA   Machado H.R., Gram L.;
RT   "Draft genome sequence of Photobacterium halotolerans S2753: a solonamide,
RT   ngercheumicin and holomycin producer.";
RL   Submitted (APR-2014) 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:KDM89942.1}.
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DR   EMBL; JMIB01000040; KDM89942.1; -; Genomic_DNA.
DR   RefSeq; WP_036756643.1; NZ_JMIB01000040.1.
DR   AlphaFoldDB; A0A066RQH1; -.
DR   STRING; 1654360.EA58_20005; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000027192; 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:SF12; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 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   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          1..76
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          133..170
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   386 AA;  41363 MW;  4A86BF6DE93A367E CRC64;
     MKSFSLPDLG EGLAESEIIE WHVKVGDVVE VDQVVLTVET AKATVEVPAP YSGTIVSRHG
     NEGDVISIGS LLMEIDETNS ADTENQEKQV AAKSKQRADA ATVVGSVSHQ SHSVNVDEFW
     VGSQVKPSAE HISALPSARA LAQKLGVNLQ KITGSGADGI IIDADVYHAC DQQLPGTEVL
     KGARRTMVGS MTESHQQIAA VTITEEALLD KWPKGEDITA RLIQAVVSAC EQEPAMNAWF
     DAETMTRCVH HKVNIGIAVD SPHGLYVPVL KDAGTLNPKA IRQWINETAE SIRARKVGRE
     EFQHATITLS NFGAIAGIYA TPVVTPPQVA IVGAGRLIEK LILVNHKPVS VRAMPLSVTF
     DHRACTGGEA ARFVKAIVEH LSKPHG
//
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