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Database: UniProt
Entry: A8UPY5_9FLAO
LinkDB: A8UPY5_9FLAO
Original site: A8UPY5_9FLAO 
ID   A8UPY5_9FLAO            Unreviewed;       453 AA.
AC   A8UPY5;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   13-SEP-2023, entry version 74.
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_05418 {ECO:0000313|EMBL:EDP69598.1};
OS   Flavobacteriales bacterium ALC-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX   NCBI_TaxID=391603 {ECO:0000313|EMBL:EDP69598.1, ECO:0000313|Proteomes:UP000003630};
RN   [1] {ECO:0000313|EMBL:EDP69598.1, ECO:0000313|Proteomes:UP000003630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALC-1 {ECO:0000313|EMBL:EDP69598.1,
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:EDP69598.1}.
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DR   EMBL; ABHI01000006; EDP69598.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8UPY5; -.
DR   STRING; 391603.FBALC1_05418; -.
DR   eggNOG; COG0508; Bacteria.
DR   OrthoDB; 9805770at2; -.
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   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:UP000003630};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EDP69598.1}.
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          128..168
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          193..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   453 AA;  49165 MW;  5550E4B4621F68BE CRC64;
     MAKFELKLPK MGESVAEATI TSWLKDIGDT IEADEAVLEI ATDKVDSEVP SEVDGVLVEK
     LFNVDDVVQV GQTIAVIETE GGDTVEVKAP ATEPVAEPEA PKAVAEVAQT VVAAKANVEP
     VISSGERFYS PLVKNIAKQE GISQNELDAI PGTGKDNRVT KNDIKNYLAS RGSTPAPVAA
     PKAEPVVEQK VNTPVTATKT PEKPAEKKSV EQPVLASGDD EIIEMSRMGK LISKYMVESV
     HTSAHVQSFI EADVTTIWNW RKKVKNDFME REGENLTFTP IFMEAVTKAL KEFPMMNISV
     QGDAIIKKKA INVGMAAALP DGNLIVPVIK NADQLNLFGM VKRVNDLANR ARLGQLSPDD
     IQGGTYTVTN VGTFGSIMGT PIINQPQVGI LALGAIRKMP AVIEGPEGDY IGIRYKMFLS
     HSYDHRVVNG ALGGQFVKYV KDYLESWDFN REI
//
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