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
//