ID F0ZCV9_DICPU Unreviewed; 509 AA.
AC F0ZCV9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=DICPUDRAFT_93881 {ECO:0000313|EMBL:EGC38204.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC38204.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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}.
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DR EMBL; GL870981; EGC38204.1; -; Genomic_DNA.
DR RefSeq; XP_003285242.1; XM_003285194.1.
DR AlphaFoldDB; F0ZCV9; -.
DR STRING; 5786.F0ZCV9; -.
DR EnsemblProtists; EGC38204; EGC38204; DICPUDRAFT_93881.
DR GeneID; 10502560; -.
DR KEGG; dpp:DICPUDRAFT_93881; -.
DR eggNOG; KOG0558; Eukaryota.
DR InParanoid; F0ZCV9; -.
DR OMA; HPCIMAP; -.
DR OrthoDB; 1399at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0016407; F:acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0031405; F:lipoic acid binding; IBA:GO_Central.
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; IPR003016; 2-oxoA_DH_lipoyl-BS.
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; PS00189; LIPOYL; 1.
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:UP000001064};
KW Transferase {ECO:0000256|RuleBase:RU003423};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 74..149
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 203..240
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 151..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 509 AA; 54948 MW; 7CBDBC41AAD9F0A7 CRC64;
MLARQIVSKR RLALQVYRNT NKTTTTSRGI STLSFTNNNN NEFKSSLPKS SSSSSLLNCK
NTFEVKRNYS SNGPILFNLA DVGEGIAECE VLTWYVKEGD SIKEFDKLCE VQSDKATVEI
TSRYDGKVTK LFHKIGGMAK VGLPLVEITP EGGASAPSPA AAPSSPSTTA APSSTPSSSS
SSKTISHHEN EITNKHGQKI KVLATPSVRH LAKANSIDLN KVQGTGKEGR VLKENILDFI
NGTNISQPLH QAKPAAPVAA PTTPAAVTPT LTLSSERESR VPISGIKKVM VKSMNAATAV
PHFGFSEEYI MDKLTELRNQ MKPMAEARGI KLSYMPFLIK ATSLALLKYP VLNSSVSPDE
SQLIYKNYHN IGVAMDTPQG LLVPNIKNVE SKSIFEIAQE LNRLQKSGIA GQLTPSDMSG
GTFSLSNIGT IGGTYCSPVL LLPEVCIGAL GKIQKLPRFD KHGNVIPQSI MIISWSGDHR
VIDGATIANF SNVLKGYIEN PNTMLFDTR
//