ID U5VXS1_9ACTN Unreviewed; 471 AA.
AC U5VXS1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=AFR_16930 {ECO:0000313|EMBL:AGZ41664.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ41664.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ41664.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ41664.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
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; CP006272; AGZ41664.1; -; Genomic_DNA.
DR RefSeq; WP_023361803.1; NC_022657.1.
DR AlphaFoldDB; U5VXS1; -.
DR STRING; 1246995.AFR_16930; -.
DR KEGG; afs:AFR_16930; -.
DR PATRIC; fig|1246995.3.peg.3435; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_11; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000017746; Chromosome.
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; 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; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000017746};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 133..170
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 98..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 48967 MW; 6F17AADA228C95F9 CRC64;
MSDRTFLLPD LGEGLTEAEV VRWLVTEGDT VAVDQPVVEV ETAKSLVEVP TPYAGRIATR
HAPEGATLEV GKPLLTVAAL VPAAETYREE EQAGSGNVLI GYGTTGASAT SRRRRPRAAL
QPAAPAAGRA PLVISPLVRR LAREGGLDLR SVTPSGPGGI ITRADVDRAL TRPSASPQAA
ESGSTRAWAP AQADDFAAAA SASPAQAADL RSTASVASAQ AAGLGSTAFA APAQAAGSVA
AAPAVAGERR IALSGFRKAV SAALTRSRAE IPEATVWVDV DATPLWELRA STPGGPGLLA
YIARFVVAGL RQYPMLNARV DTERQEIVEF ERVNLGIAVQ GERGLVVPAV MDAGNRTTAQ
LDEEIRRVTA SAREGRATAQ ELSAGTFTLN NYGSFNVDGS AAIINHPQVA ILGFGRIIDR
PWVVGGEVCV RKITQMSFVF DHRVCDGGTA AGFMRSVADA IEDPASAIAR L
//
