ID A0A090Q222_9FLAO Unreviewed; 447 AA.
AC A0A090Q222;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=JCM19294_1755 {ECO:0000313|EMBL:GAK96242.1};
OS Nonlabens tegetincola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=323273 {ECO:0000313|EMBL:GAK96242.1, ECO:0000313|Proteomes:UP000029221};
RN [1] {ECO:0000313|EMBL:GAK96242.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19294 {ECO:0000313|EMBL:GAK96242.1};
RA Nakanishi M., Meirelles P., Suzuki R., Takatani N., Mino S., Suda W.,
RA Oshima K., Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L.,
RA Niwa A., Sawabe T., Sawabe T.;
RT "Draft Genome Sequences of Marine Flavobacterium Nonlabens Strains NR17,
RT NR24, NR27, NR32, NR33, and Ara13.";
RL Genome Announc. 2:e01165-14(2014).
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:GAK96242.1}.
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DR EMBL; BBML01000002; GAK96242.1; -; Genomic_DNA.
DR RefSeq; WP_042277423.1; NZ_BBML01000002.1.
DR AlphaFoldDB; A0A090Q222; -.
DR STRING; 319236.BST91_08940; -.
DR eggNOG; COG0508; Bacteria.
DR Proteomes; UP000029221; 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 ECO:0000313|EMBL:GAK96242.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000029221};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:GAK96242.1}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 135..175
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 82..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 47603 MW; 5E37DCC4C5C39566 CRC64;
MATFELKLPK MGESVAEATI TTWLKNVGDT IEMDEPVLEI ATDKVDSEVP SEVDGVLKEI
LFQVDDVVQV GQTIAIIETD GDSATDAASS SSNDSTPAEA TAQPVEAVKA ATAQVDRGMA
TAGKVDNDYA NSDSFYSPLV KNIAKEENIS LEELEAINGT GKDGRVTKND ILAYVEDKKA
GKTAPAPAAA PTAAASKPAA APVKAAPVSV NGEDEIIEMS RMGKLISHHM IASVQTSAHV
QSFIEADVTT IWNWRKKNKD AFKAREGENL TFTPIFMEAV ATALKEFPMM NISVDGDKII
KRKNVNLGMA AALPDGNLIV PVIKNADQLN LVGMAKSVND LANRARNGKL KPDDTQGGTY
TVTNVGTFGS VLGTPIINQP QVGILALGAI RKVPAVIETP DGDFIGVRMK MFLSHSYDHR
VVNGALGGQF VQRVAQLLES FDPNRTI
//
