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Database: UniProt
Entry: A0A2S5AAM0_9FLAO
LinkDB: A0A2S5AAM0_9FLAO
Original site: A0A2S5AAM0_9FLAO 
ID   A0A2S5AAM0_9FLAO        Unreviewed;       433 AA.
AC   A0A2S5AAM0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
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=C3L50_10805 {ECO:0000313|EMBL:POY39641.1};
OS   Flavobacterium alvei.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2080416 {ECO:0000313|EMBL:POY39641.1, ECO:0000313|Proteomes:UP000237310};
RN   [1] {ECO:0000313|EMBL:POY39641.1, ECO:0000313|Proteomes:UP000237310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HR-AY {ECO:0000313|EMBL:POY39641.1,
RC   ECO:0000313|Proteomes:UP000237310};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) 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:POY39641.1}.
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DR   EMBL; PQVG01000005; POY39641.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S5AAM0; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000237310; 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   Reference proteome {ECO:0000313|Proteomes:UP000237310};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          124..164
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   433 AA;  47373 MW;  6D5F92BDB224153A CRC64;
     MARFELKLPK MGESVAEATI TNWLKQVGDK IEADETVLEV ATDKVDSELP SEVSGILVEQ
     LFAKDDIVQV GQTIAIIETE GISVSNEPKQ EIVAPVEVAA IEKTIEVVKE TLAVPTNFSD
     SEKFFSPLVK NIAKEEGISL AELENITGSG KEGRVTKEDI LGYVAARKLD TRTNIQEPLA
     QQRTTNNEQP KIPVSVNGGD EIIEMDRMRK LISGYMMASI QTSAHVQSFI EVDVTNIVKW
     RDKVKTAFEK REGEKLTYTP IFMEAVAKAL KDFPMMNIAV DGDKIIKRKN INLGMAAALP
     NGNLIVPVIK NADQLNLVGM AKAVNDLGNR AKLGKLKPDD TQGGTYTVTN VGTFGSVFGT
     PIINQPEVGI LALGAIRKVP AVIETPEGDF IGIRQKMFLS HSYDHRVVDG ALGGSFVKRV
     AEYLEAFDLD RNF
//
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