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Database: UniProt
Entry: A0A1G6TYV7_9SPHI
LinkDB: A0A1G6TYV7_9SPHI
Original site: A0A1G6TYV7_9SPHI 
ID   A0A1G6TYV7_9SPHI        Unreviewed;       505 AA.
AC   A0A1G6TYV7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=SAMN05216464_101448 {ECO:0000313|EMBL:SDD33547.1};
OS   Mucilaginibacter pineti.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1391627 {ECO:0000313|EMBL:SDD33547.1, ECO:0000313|Proteomes:UP000199072};
RN   [1] {ECO:0000313|EMBL:SDD33547.1, ECO:0000313|Proteomes:UP000199072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47C3B {ECO:0000313|EMBL:SDD33547.1,
RC   ECO:0000313|Proteomes:UP000199072};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNAI01000001; SDD33547.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6TYV7; -.
DR   STRING; 1391627.SAMN05216464_101448; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000199072; 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:UP000199072};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:SDD33547.1}.
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          155..195
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          243..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   505 AA;  54219 MW;  B3924B24E1861B08 CRC64;
     MAKYQLLLPK MGESVAEATI IKWTKNPGDH VDADEAVMEI ATDKVDSDVP SPVAGKLIEQ
     LYKENDVVQV GAVIAIIETA EEEAVEVAPV TVAAPATEEK IEEQPPVVEE ASAVTAPEIT
     EQEPDTPAPV DIPGLAQLEQ TAQPVQEAFK SEGRFYSPLV RNIASQEGIR VAELDTIPGT
     GAEGRLTKDD LLSYLQNRQN PTAAKPPVFE EQIKAPVAQN TAEPAAVPVP VPLTDAEPAA
     VEAAEGKAPI AEKAAAPQPT ASQPGTSVSG GDEIIEMDRM RRLIADHMVM SKQTSPHVTS
     FVEADVTSLV LWREKVKNSF EKREGEKITF TPIFIEAVVK AIKDFPMINV TVNGTQIIKK
     ANINISMATA LPSGNLIVPV IKKADELSLL GITKAVNDLA NRARIGKLLP DDVRDGTFTI
     TNVGSFGNVM GTPIINQPQV AILAVGAIKK KPAVIETPEG DAIAIRHMMF LSLSYDHRVV
     DGALGGSFVR RVADYLEKWD PNRVI
//
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