ID A0A0M8M8D1_9FLAO Unreviewed; 438 AA.
AC A0A0M8M8D1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=AM493_00200 {ECO:0000313|EMBL:KOS04635.1};
OS Flavobacterium akiainvivens.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1202724 {ECO:0000313|EMBL:KOS04635.1, ECO:0000313|Proteomes:UP000037755};
RN [1] {ECO:0000313|EMBL:KOS04635.1, ECO:0000313|Proteomes:UP000037755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IK-1 {ECO:0000313|EMBL:KOS04635.1,
RC ECO:0000313|Proteomes:UP000037755};
RA Wan X., Hou S., Saito J., Donachie S.;
RT "Whole genome sequence of Flavobacterium akiainvivens IK-1T, from decaying
RT Wikstroemia oahuensis, an endemic Hawaiian shrub.";
RL Submitted (AUG-2015) 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:KOS04635.1}.
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DR EMBL; LIYD01000005; KOS04635.1; -; Genomic_DNA.
DR RefSeq; WP_054405612.1; NZ_LIYD01000005.1.
DR AlphaFoldDB; A0A0M8M8D1; -.
DR STRING; 1202724.AM493_00200; -.
DR PATRIC; fig|1202724.3.peg.31; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000037755; 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:UP000037755};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 125..165
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 169..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 438 AA; 47200 MW; 05147426AB65D1F2 CRC64;
MAKFELKLPK MGESVAEATI TNWLKKVGDH IAADEAVLEI ATDKVDSEVP SEVSGTLTEI
FFKENDVVQV GQTIAHIETE GGVVVDAPSE ATPAVTENIQ AIEKTVTAAK EAVATPEDFS
GSEKFFSPLV KNIAKEEGVT LAELESINGT GKDGRVTKDD ILGYVKEKSQ NPNAKSQTVA
ANSQPATLNP QPQTPKAAPS VNGQDEIVEM DRMRKLISGY MVQSVQTSAH VQSFIEVDVT
NIVKWRDKVK TAFEKREGEK LTFTPIFMEA VAKALKDFPG MNISVDGEYI IKKKNINLGM
AAALPNGNLI VPVIKNADQL NLVGMAKAVN DLGNRAKAGK LKPDDTQGGT YTVTNVGTFG
SVFGTPIINQ PQVGILALGA IRKVPAVIET PDGDFIGIRQ KMFLSHSYDH RVVDGALGGS
FVKRVAEYLE AFDPKRDF
//
