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Database: UniProt
Entry: J8W4B4_9PORP
LinkDB: J8W4B4_9PORP
Original site: J8W4B4_9PORP 
ID   J8W4B4_9PORP            Unreviewed;       433 AA.
AC   J8W4B4;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
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=HMPREF1323_0072 {ECO:0000313|EMBL:EJU15178.1};
OS   Porphyromonas sp. oral taxon 279 str. F0450.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=1125723 {ECO:0000313|EMBL:EJU15178.1, ECO:0000313|Proteomes:UP000004156};
RN   [1] {ECO:0000313|EMBL:EJU15178.1, ECO:0000313|Proteomes:UP000004156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0450 {ECO:0000313|EMBL:EJU15178.1,
RC   ECO:0000313|Proteomes:UP000004156};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JUL-2012) 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:EJU15178.1}.
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DR   EMBL; ALKJ01000051; EJU15178.1; -; Genomic_DNA.
DR   RefSeq; WP_009433826.1; NZ_ALKJ01000051.1.
DR   AlphaFoldDB; J8W4B4; -.
DR   PATRIC; fig|1125723.3.peg.1710; -.
DR   Proteomes; UP000004156; 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; IPR021630; Rpf1_C.
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; PF11574; Rpf1_C; 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:EJU15178.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004156};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EJU15178.1}.
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          121..161
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          87..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   433 AA;  46238 MW;  50AF66FC42D545CA CRC64;
     MATFDIKMPK MGESVTECTI TVLNVKVGDY IEEDTDLFEI TSAKTAATIP SPVAGTIVKI
     NYAEGDTVAV GEPVIIVDTS GQAVAPATPA PAAEKEAPAP AAAPTPSIPV TEVHRGTVER
     WYSPVVLERA KAAKVSQEEL DKIQGTGFGG RVSKADIVRY IEQKKGAPAP TPRAERAAAP
     APASAARPQV AAPAVPVGPE DRVIPMDPIR RIIADRMVQS VQVAPHVTSF IKADITDLVK
     WREAEKDSFK KREGYSLTYM SPVIEAVARA LKDFPRINAA VDGYNIIERK HVNVGMAVAL
     PDGNLVVPVI RDADKLSLAG IAEQVARLAD KSRKGQLTPD EMSGGTFTIS NYGSSGTLFG
     TPIINQPESA ILGIGAIEKE PTILETPAGD VIAVRHKIYL SFSYDHRIID GMLGGAFLQA
     VARYLEEWKT NNA
//
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