ID A0A1N6U493_9BACI Unreviewed; 455 AA.
AC A0A1N6U493;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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=SAMN05443094_103158 {ECO:0000313|EMBL:SIQ60357.1};
OS Domibacillus enclensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1017273 {ECO:0000313|EMBL:SIQ60357.1, ECO:0000313|Proteomes:UP000186385};
RN [1] {ECO:0000313|EMBL:SIQ60357.1, ECO:0000313|Proteomes:UP000186385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIO-1016 {ECO:0000313|EMBL:SIQ60357.1,
RC ECO:0000313|Proteomes:UP000186385};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; FTLX01000003; SIQ60357.1; -; Genomic_DNA.
DR RefSeq; WP_045851489.1; NZ_MWSK01000003.1.
DR AlphaFoldDB; A0A1N6U493; -.
DR STRING; 1017273.SAMN05443094_103158; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000186385; 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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:SIQ60357.1};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:SIQ60357.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 147..184
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 86..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 48731 MW; A9CE0FF14DEC2AD3 CRC64;
MAFEFKLPDI GEGIHEGEIV KWFVKPGDQV AEDDVLCEVQ NDKAVVEIPS PVAGTVEEVL
VDEGATAIVG DTLIKFDAPG YEDLKFKGDD HGDGEEKTEE QVQATAEAGQ NVDKAPADAP
AKEEAPAQST GAGSQPQAEV DPNRRIIAMP SVRKYAREKD VNIGLVEGSG KNGRITKDDI
DSFLSGGQTS AAPAQEDAAV QQDAPAAKEE SKPAAASIPE GEYPETREKM SGIRKAIAKA
MVNSKHTAPH VTLMDEVEVT ELWAHRKKFK DIAAEKGVKL TFLPYVVKAL TSALKEYPAF
NTSIDDATNE IVHKHYYNIG IAADTEKGLM VPVVKNADRK SMFAISDEIN ELAGKARDGK
LAPAEMKGAS CTITNIGSAG GQWFTPVINH PEVAILGIGR IAEKAIVKNG EIVAAPVLAL
SLSFDHRMID GATAQNALNH IKRLLNNPEL LLMEA
//
