ID A0A0M8VEJ7_9ACTN Unreviewed; 692 AA.
AC A0A0M8VEJ7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=ADL01_31790 {ECO:0000313|EMBL:KOV61053.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV61053.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV61053.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV61053.1,
RC ECO:0000313|Proteomes:UP000037738};
RA Noorani M.;
RL Submitted (JUL-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 -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KOV61053.1}.
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DR EMBL; LGDW01000455; KOV61053.1; -; Genomic_DNA.
DR RefSeq; WP_053745452.1; NZ_LGDW01000455.1.
DR AlphaFoldDB; A0A0M8VEJ7; -.
DR PATRIC; fig|1519490.3.peg.6926; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000037738; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR CDD; cd06849; lipoyl_domain; 1.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like 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; IPR011053; Single_hybrid_motif.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 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:UP000037738};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 345..420
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 425..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 692 AA; 72954 MW; 6CD73FE764EDE806 CRC64;
MAATMAQALN TALRDALTAD ERVVVFGEDV GRLGGVFRVT DGLADTFGDR RCFDTPVAEA
GIAGLAVGMA MAGFRPVVEM QFDAFAYPAF EQIASHVAKF RNRTRGTLAL PMVVRIPYGG
GIGGVEHHSD SSEAYYAHTA GLKVVTPATV GDAYSLLREA IEDPDPVVFL EPKRHYWTKE
DIQLPLTTSP FGTAAVRRPG TDATLVAYGP SVAVALAAAR EAVAEGLDVE VLDLRTLVPL
DDHALTASVR RTGRCLVVHE SQGFAGVGAE IAARVQERCF DALRAPVLRV TGLDIPYPPP
LLEDAHLPGV GRVLAGLRRL LPDGGQGGRR PTPVSLTEVE PAPGDRTFLL PDLGEGLAEA
EVLEWTVAVG DSVTHDQPVV EVETAKSVVA LPTPFAGTVT ALHCRAGEIV EVGAPLLSVA
EAAPEGDSGA VLTGYGTGGA RRATRNGVAP AQHTSQNQPQ SRPQNRPVNN GPSAAPADRQ
PGLRLPLDAV AEKFARTHRD TPAVTIWADA DATALLAARD TLGTGLLPLL ARAALTGLAA
FPALNARVDD ARSEIVRLPQ VHLGFAAQTD DGLVVPVVRD ADRLPLDDLA TELRRLTGLA
RRGALPVEHR TGGTFTLNNY GVLGVDGATP LLNHPQTAML SIGRLVERPW AVNGRVEVRE
IVHLSLTFDH RVCDGGTAAG FLRHVIDGIT AP
//
