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Database: UniProt
Entry: C1G4D1_PARBD
LinkDB: C1G4D1_PARBD
Original site: C1G4D1_PARBD 
ID   C1G4D1_PARBD            Unreviewed;       495 AA.
AC   C1G4D1;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 2.
DT   24-JAN-2024, entry version 62.
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=PADG_01797 {ECO:0000313|EMBL:EEH45647.2};
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH45647.2, ECO:0000313|Proteomes:UP000001628};
RN   [1] {ECO:0000313|EMBL:EEH45647.2, ECO:0000313|Proteomes:UP000001628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18 {ECO:0000313|EMBL:EEH45647.2,
RC   ECO:0000313|Proteomes:UP000001628};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(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; KN275958; EEH45647.2; -; Genomic_DNA.
DR   RefSeq; XP_010757076.1; XM_010758774.1.
DR   AlphaFoldDB; C1G4D1; -.
DR   STRING; 502780.C1G4D1; -.
DR   GeneID; 22581395; -.
DR   KEGG; pbn:PADG_01797; -.
DR   VEuPathDB; FungiDB:PADG_01797; -.
DR   eggNOG; KOG0558; Eukaryota.
DR   HOGENOM; CLU_016733_10_0_1; -.
DR   InParanoid; C1G4D1; -.
DR   OMA; HPCIMAP; -.
DR   OrthoDB; 1399at2759; -.
DR   Proteomes; UP000001628; 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:UP000001628};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          50..125
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          192..229
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          239..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   495 AA;  53532 MW;  9D38A5EA567E3C26 CRC64;
     MMALRCRGSL TQALRPICSA SRLLPAAARI YPISSPRQRF FHGSPASWAI RSQVLKDVGE
     GITEIQIIQW YVQEGAKIEE WKPLCQYQSD KAVDDITSRY EGVIKKLHFQ ADETVPTGMA
     LCDIDVDESK YPVENATPPP AIKPAATPPL PLEQQQVKQE VKEGSAISLN TAEAPPKPVE
     QPATLKSKYA TLATPAVRGM LKGLNVDILN VTGTGKDGRV IKEDVLRYVA ERDAGAVEVT
     ASSSATPQSP PAALGISTPQ TETSTPLTSI QSQMFKTMTR SLSIPHFLYA DELNIASLSS
     IRKKLASHPT HPQKLSYLPF IIKAVSLSLN TFPLLNARVD TTNPNKPSLI MRSNHNIGVA
     MDTPTGLLVP NIKNVQARSI LDIATELVRL TEVARAGKLT PADLNGGTIT VSNIGNIGGT
     YVGPVIVPNE VAILGIGRAK IVPVFDKAGN VVKGEKVNFS WSADHRVVDG ATMARMADRV
     RGYLEEPELM MLALR
//
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