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Database: UniProt
Entry: A0A101P5P2_9ACTN
LinkDB: A0A101P5P2_9ACTN
Original site: A0A101P5P2_9ACTN 
ID   A0A101P5P2_9ACTN        Unreviewed;       589 AA.
AC   A0A101P5P2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=AQI95_15650 {ECO:0000313|EMBL:KUN05372.1};
OS   Streptomyces yokosukanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67386 {ECO:0000313|EMBL:KUN05372.1, ECO:0000313|Proteomes:UP000053127};
RN   [1] {ECO:0000313|EMBL:KUN05372.1, ECO:0000313|Proteomes:UP000053127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40224 {ECO:0000313|EMBL:KUN05372.1,
RC   ECO:0000313|Proteomes:UP000053127};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces yokosukanensis DSM 40224, type
RT   strain for the species Streptomyces yokosukanensis.";
RL   Submitted (OCT-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   -!- 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:KUN05372.1}.
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DR   EMBL; LMWN01000020; KUN05372.1; -; Genomic_DNA.
DR   RefSeq; WP_067123277.1; NZ_KQ948211.1.
DR   AlphaFoldDB; A0A101P5P2; -.
DR   STRING; 67386.AQI95_15650; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000053127; Unassembled WGS sequence.
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; 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; 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|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053127};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:KUN05372.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          127..202
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          282..319
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          251..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..266
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   589 AA;  58509 MW;  4E74863FD6E97157 CRC64;
     MAVSVTLPAL GESVTEGTVT RWLKAEGERV EADEPLLEVS TDKVDTEIPS PASGVLASIK
     VAEDETVEVG AELAVIDDGT GAPAAAPAPA AAEAPAPAAP VAAPAPVAEA PAAPAAAPAA
     PAGGATGTDV VLPALGESVT EGTVTRWLKS VGDSVEADEP LLEVSTDKVD TEIPAPASGV
     LLEIVVGEDE TAEVGAKLAV IGAPGAAPAA APAPAAPAPA PVAAAPAPVA PAAPVAPAPA
     PAVPAAAAPV APAAPAPAPA PVVPATAPSS PTATQATDEG AYVTPLVRKL AAENGVDLAA
     VKGTGVGGRI RKQDVIAAAE AAKAAATAPA PAAAAAPAAA KKAPALEVSP LRGQTVKMTR
     IRKVIGDNMV KALHEQAQLS SVVEVDVTRL MKLRAKAKDG FAAREGVKLS PMPFFVKAAA
     QALKAHPVIN ARINEAEGTI TYFDTENIGI AVDSEKGLMT PVIKGAGDLN IAGISKATAD
     LAGKVRANKI TPDELSGATF TISNTGSRGA LFDTIIVPPN QVAILGIGAT VKRPAVIETE
     EGTVIGVRDM TYLTLSYDHR LVDGADAARY LTAVKAILEA GEFEVELGL
//
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