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Database: UniProt
Entry: A0A085EFZ4_9FLAO
LinkDB: A0A085EFZ4_9FLAO
Original site: A0A085EFZ4_9FLAO 
ID   A0A085EFZ4_9FLAO        Unreviewed;       437 AA.
AC   A0A085EFZ4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-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=FEM08_30940 {ECO:0000313|EMBL:KFC58139.1};
OS   Flavobacterium gilvum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1492737 {ECO:0000313|EMBL:KFC58139.1, ECO:0000313|Proteomes:UP000028636};
RN   [1] {ECO:0000313|EMBL:KFC58139.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EM1308 {ECO:0000313|EMBL:KFC58139.1};
RA   Shin S.-K., Yi H.;
RT   "Genome Sequence of Flavobacterium sp. EM1308.";
RL   Submitted (MAY-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   -!- 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:KFC58139.1}.
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DR   EMBL; JNCP01000115; KFC58139.1; -; Genomic_DNA.
DR   RefSeq; WP_035640047.1; NZ_JNCP01000115.1.
DR   AlphaFoldDB; A0A085EFZ4; -.
DR   STRING; 1492737.EM308_16720; -.
DR   KEGG; fgl:EM308_16720; -.
DR   PATRIC; fig|1492737.3.peg.3078; -.
DR   eggNOG; COG0508; Bacteria.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000028636; 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   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          122..162
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   437 AA;  47191 MW;  1B02492E1175BE9F CRC64;
     MARFELKLPK MGESVAEATI TNWLKEVGDK IEADDAVLEI ATDKVDSEVP SEVSGILVEK
     LFGKDDLVQV GQTIAIIETE AVEAGSPRPE VAPAIVEEIL KTVEVAKETV ATPISFSESD
     KFFSPLVKNI AKEEGITLDE LQSIAGSGKE GRVTKDDILD YIKNRSLQPA NAVATPTKEV
     ETLKVVSAEA PSQAAAPASV NGADEIVEMD RMRKLISGYM VASIQTSAHV QSFIEVDVTN
     IVKWRDKVKN AFEKREGEKL TYTPIFMEAV AKALKDFPGM NISVEGDFII KKKNINIGMA
     AALANGNLIV PVIKNADQLN LVGMAKAVND LGNRAKANKL KPDDTQGGTY TVTNVGTFGS
     VFGTPIINQP QVGILALGAI RKVPAVIETP DGDFIGIRQK MFLSHSYDHR VVDGALGGSF
     VKRVAEYLEA FDVNRDY
//
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