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Database: UniProt
Entry: A8UDZ6_9FLAO
LinkDB: A8UDZ6_9FLAO
Original site: A8UDZ6_9FLAO 
ID   A8UDZ6_9FLAO            Unreviewed;       447 AA.
AC   A8UDZ6;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   22-FEB-2023, entry version 75.
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=FBALC1_14167 {ECO:0000313|EMBL:EDP72253.1};
OS   Flavobacteriales bacterium ALC-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX   NCBI_TaxID=391603 {ECO:0000313|EMBL:EDP72253.1, ECO:0000313|Proteomes:UP000003630};
RN   [1] {ECO:0000313|EMBL:EDP72253.1, ECO:0000313|Proteomes:UP000003630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALC-1 {ECO:0000313|EMBL:EDP72253.1,
RC   ECO:0000313|Proteomes:UP000003630};
RA   Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2007) 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:EDP72253.1}.
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DR   EMBL; ABHI01000001; EDP72253.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8UDZ6; -.
DR   STRING; 391603.FBALC1_14167; -.
DR   eggNOG; COG0508; Bacteria.
DR   Proteomes; UP000003630; Unassembled WGS sequence.
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   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:UP000003630};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EDP72253.1}.
FT   DOMAIN          16..91
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          143..183
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          98..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  49537 MW;  7E6C607F414D0B28 CRC64;
     MLLIFISKII RNRLKEFELK MPKMGESITE GTIINWLISE GDTFEEGDII LEVATDKVDN
     EVPAPASGTL VKTLFQAKDI VPVGEVMAIL EVSEEKKLNP NSNSNKETKA VSSSAVENKA
     KQKNLKASNS SSTSFSTSNA NTFFSPLIIS IAKEQHISFE ELARIPATGN EGRLRKSDLF
     QYIEDGRPFK FAQPITQDPT AYRIPQLTFE KGKGKIVEMD RMRQMIADHM VYSKHTSPHV
     TAYVEADLTN MVNWRNANKK AFQEKYDERL TFTPLFVEAV AKAVKDFPNI NASVDGTNII
     VKEDINIGMA TALPSGNLIV PVVKNADTKD LKTIASDVNE LAGKARENKL SGDDIKGSTF
     TISNVGTFGS VMGTPIINQP EVAILALGII KKRPEVITTE KGDEIAIRSM MYLSLSFDHR
     VVDGFLGGSF VRRVADYFEQ FDINRKI
//
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