ID   A0A2Z4US23_9ACTN        Unreviewed;       589 AA.
AC   A0A2Z4US23;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
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:AWZ11220.1};
GN   ORFNames=DRB96_01470 {ECO:0000313|EMBL:AWZ11220.1};
OS   Streptomyces sp. ICC1.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2099583 {ECO:0000313|EMBL:AWZ11220.1, ECO:0000313|Proteomes:UP000250268};
RN   [1] {ECO:0000313|EMBL:AWZ11220.1, ECO:0000313|Proteomes:UP000250268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICC1 {ECO:0000313|EMBL:AWZ11220.1,
RC   ECO:0000313|Proteomes:UP000250268};
RA   Gosse J.;
RT   "Whole genome sequencing and metabolomic study of cave Streptomyces
RT   isolates ICC1 and ICC4.";
RL   Submitted (JUN-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; CP030287; AWZ11220.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z4US23; -.
DR   Proteomes; UP000250268; 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:UP000250268};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AWZ11220.1}.
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          286..323
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   589 AA;  58372 MW;  4EFEA8CDE60C3DE2 CRC64;
     MSVSVTLPAL GESVTEGTVT RWLKAEGERV EADEPLLEVS TDKVDTEIPS PVSGILASIK
     VAEDETVEVG AELAIIDDGS GAPAAAAAPA AEAPAAAAPA AAAPVAEAPA APAPVAEAPA
     APAAAAAPAA GTDVVLPALG ESVTEGTVTR WLKQVGESVE ADEPLLEVST DKVDTEIPAP
     VAGVLLEILV AEDENAEVGA RLAVIGVAGA APAAAPAAAA PAPAAAPAPA AAPVAAPVAA
     PAPVVAAPAV AAPVAAPAPV AAPAPVAPVA PAAPAAPVSA GDEGAYVTPL VRKLASESGV
     DLSSVAGTGV GGRIRKQDVL AAAEAAKAAA AAPAATAAPA AKAPAAAVSE LRGQTVKMTR
     MRKVIGDNMM KALHSQAQLS SVVEVDITKI MKLREKAKAG FLAREGVKLS PMPFFVKAAA
     QALKAHAVVN ARINEDEGTI TYFDSENIGI AVDSEKGLMT PVIKGAGGLN LAGISKATAE
     LASKVRGNKI TPDELSGATF TISNTGSRGA LFDTVIVPPN QVAILGIGAT VKRPVVIETP
     EGTNIGIRDM TYLTLSYDHR LVDGADAARY LSAVKSILEA GEFEVELGL
//