ID A0A1R0GV64_9FUNG Unreviewed; 484 AA.
AC A0A1R0GV64;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=AYI68_g5092 {ECO:0000313|EMBL:OLY80806.1};
OS Smittium mucronatum.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133383 {ECO:0000313|EMBL:OLY80806.1, ECO:0000313|Proteomes:UP000187455};
RN [1] {ECO:0000313|EMBL:OLY80806.1, ECO:0000313|Proteomes:UP000187455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALG-7-W6 {ECO:0000313|EMBL:OLY80806.1,
RC ECO:0000313|Proteomes:UP000187455};
RX PubMed=27343289; DOI=10.1093/molbev/msw126;
RA Wang Y., White M.M., Kvist S., Moncalvo J.M.;
RT "Genome-Wide Survey of Gut Fungi (Harpellales) Reveals the First
RT Horizontally Transferred Ubiquitin Gene from a Mosquito Host.";
RL Mol. Biol. Evol. 33:2544-2554(2016).
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:OLY80806.1}.
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DR EMBL; LSSL01003111; OLY80806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R0GV64; -.
DR STRING; 133383.A0A1R0GV64; -.
DR Proteomes; UP000187455; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:RHEA.
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 ECO:0000313|EMBL:OLY80806.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000187455};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:OLY80806.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 26..105
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 180..217
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 484 AA; 53078 MW; AEC05F65A1C5489A CRC64;
MSLIPSLTFK IAPRPILFKK FSVYNYNRIV VPYKLADIGE GITECEIIQW YIKVGDKVAQ
FDKICEVQSD KATVEITSRY DGVIKELFYA ENEMAIVGTP LLSIDLDESA EAPAGTAPIS
VEDYSQQCDT NIPETLLKSE TDSVAGNTTA TIPQIQTSYN GHGNTESMEE HTGLSNEPIH
STPAVRFLAK ERGINLSKVK GTGKNGRITK EDLFSFSEQK TARDSVQPTT QQPVLNETQS
ESSIVKLTSI QRAMFKSMTA SLSIPHFGLS EEIEMDEIIK HRTEINKFLL ETLHPVGKVS
FLPFFIKAAS MSLSQYPIIN AKLVVSGRDG QPLKEPHLVY NQSHNIGIAI DTKIGLLVPN
IKDVQSKSIL DISSEIQSLI KQANSGSLSV DTLKNSTFTI SNVGNIGSST VLSPVIVPDQ
VSIGAFGKIS TVPRFVDSVV VPKSVLLANW RADHRVIDGA TLARFSSHFK LLLEHPAIMA
ANMR
//
