ID K5VCI8_PHACS Unreviewed; 519 AA.
AC K5VCI8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=PHACADRAFT_246690 {ECO:0000313|EMBL:EKM60651.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM60651.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM60651.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM60651.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylpropanoyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-
CC [protein] = CoA + N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:18865, Rhea:RHEA-COMP:10475,
CC Rhea:RHEA-COMP:10497, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338,
CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83142; EC=2.3.1.168;
CC Evidence={ECO:0000256|ARBA:ARBA00035973};
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH930468; EKM60651.1; -; Genomic_DNA.
DR RefSeq; XP_007390099.1; XM_007390037.1.
DR AlphaFoldDB; K5VCI8; -.
DR STRING; 650164.K5VCI8; -.
DR GeneID; 18913879; -.
DR KEGG; pco:PHACADRAFT_246690; -.
DR HOGENOM; CLU_016733_10_0_1; -.
DR InParanoid; K5VCI8; -.
DR OrthoDB; 1399at2759; -.
DR Proteomes; UP000008370; Unassembled WGS sequence.
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:UP000008370};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 35..110
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 180..218
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 114..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 56081 MW; 7839A960D2D529BA CRC64;
MLGRLVRLRG RSLRPATVYG VSHLHSSAVC WGKVLRTFKL ADIGEGITEC EVIRWNVSPS
SQVAAFDALC EVQSDKASVE ITSPFDGVVK DLLVKESEVA KVGEGLCIIE VDEEHAGDEQ
TSSPPPHPEQ EAMESKDFSA ERNVEPTADV PTPVRRHHPL DPSAPQDVKA TLGTNAENVL
ATPATRYFAR QNGVDLAKLA PGSGKGGRIE RRDVEAYLAG GQERNAVPIT QAPPQVQQAE
DAVIELGRTR YGMWKAMTKS LEIPHFGYST SLDLTTLNEI MPILNSYIPA HYLPPSSKPS
HPPAVSPSAF YAQSSPPTAE PSAQFTKLTY LPILLKTLSR AMLEWPLFRS SIMPSWNAAS
GEKPTLTLRS HADINIALST PTGLYTPTLQ RVDAHNVYAL AAQLKHLSHL GRQIPCGLTP
AEMPKRGGTL TVSNVGGIGD GEAASPVLVP GGGVAIVAIG RARWVWDVNR GDGRGERRLK
VGVSWSADHR VVEGAELVAF IESWRSWVEA PQRLIAEGV
//