ID A0A3S8X0L4_9ACTN Unreviewed; 590 AA.
AC A0A3S8X0L4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=sucB {ECO:0000313|EMBL:AZM62702.1};
GN ORFNames=DLM49_27035 {ECO:0000313|EMBL:AZM62702.1};
OS Streptomyces sp. WAC 01438.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2203204 {ECO:0000313|EMBL:AZM62702.1, ECO:0000313|Proteomes:UP000271045};
RN [1] {ECO:0000313|EMBL:AZM62702.1, ECO:0000313|Proteomes:UP000271045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC 01438 {ECO:0000313|EMBL:AZM62702.1,
RC ECO:0000313|Proteomes:UP000271045};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-2018) 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; CP029601; AZM62702.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S8X0L4; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000271045; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
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; IPR014276; 2-oxoglutarate_DH_E2.
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 NCBIfam; TIGR02927; SucB_Actino; 1.
DR PANTHER; PTHR43416:SF8; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
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; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000271045};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AZM62702.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 131..206
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 284..321
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 78..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..114
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 59163 MW; 287E68EA0D031424 CRC64;
MAVSVTLPAL GESVTEGTVT RWLKAEGERV EADEPLLEVS TDKVDTEIPA PASGVLSSIK
VAEDETVEVG AELALIDDGS GAPAATPAPA AEQAAPPAPA PEPQAQPSTE QPAPAPAPSA
EATAGGGSAQ GTDVALPALG ESVTEGTVTR WLKSVGDTVE ADEPLLEVST DKVDTEIPAP
ASGTLLEIVV GEDETAEVGA KLAVIGEAGA APAAAPAPAA PEAPAQPAPA PAPAAPAPAP
TPTPAPAPAP QPAAPAPAPT PAPAPQAPAA PAPAAARATD EGAYVTPLVR KLAAENGVDL
STVKGTGVGG RIRKQDVIAA AEAAKAAAPA PAAAPAAAPA AKKAPVLEAS PLRGQTVKMP
RIRKVIGDNM VKALHEQAQL SSVVEVDVTR LMKLRALAKD AFAAREGVKL SPMPFFVKAA
AQALKAHAPI NARINEAEGT ITYFDTENIG IAVDSEKGLM TPVIKNAGDL NLAGIAKATA
ELAGKVRGNK ITPDELSGAT FTISNTGSRG ALFDTIIVPP GQVAILGIGA TVKRPAVIES
EEGTAIGIRD MTYLTLSYDH RLVDGADAAR YLTAVKAILE AGEFEVELGL
//
