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Database: UniProt
Entry: A0A0G4NYV2_PENCA
LinkDB: A0A0G4NYV2_PENCA
Original site: A0A0G4NYV2_PENCA 
ID   A0A0G4NYV2_PENCA        Unreviewed;       484 AA.
AC   A0A0G4NYV2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   05-JUN-2019, entry version 22.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   ORFNames=PCAMFM013_S002g001044 {ECO:0000313|EMBL:CRL19174.1};
OS   Penicillium camemberti FM 013.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1429867 {ECO:0000313|EMBL:CRL19174.1, ECO:0000313|Proteomes:UP000053732};
RN   [1] {ECO:0000313|EMBL:CRL19174.1, ECO:0000313|Proteomes:UP000053732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FM 013 {ECO:0000313|Proteomes:UP000053732};
RX   PubMed=24407037; DOI=10.1038/ncomms3876;
RA   Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA   Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F.,
RA   Goarin A., Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T.,
RA   Brygoo Y.;
RT   "Multiple recent horizontal transfers of a large genomic region in
RT   cheese making fungi.";
RL   Nat. Commun. 5:2876-2876(2014).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2).
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA =
CC         (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC         COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12;
CC         Evidence={ECO:0000256|RuleBase:RU361137};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU361137};
CC       Note=Binds 1 lipoyl cofactor covalently.
CC       {ECO:0000256|RuleBase:RU361137};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361137}.
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DR   EMBL; HG793135; CRL19174.1; -; Genomic_DNA.
DR   EnsemblFungi; CRL19174; CRL19174; PCAMFM013_S002g001044.
DR   Proteomes; UP000053732; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 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; IPR006257; LAT1.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR01349; PDHac_trf_mito; 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:RU361137};
KW   Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:CRL19174.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053732};
KW   Ligase {ECO:0000313|EMBL:CRL19174.1};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053732};
KW   Transferase {ECO:0000256|RuleBase:RU361137}.
FT   DOMAIN       58    134       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      201    238       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION      149    199       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0G4NYV2}.
SQ   SEQUENCE   484 AA;  51470 MW;  7125F311DE87C245 CRC64;
     MVASAIRMRT PSAMFMSRGA AAMRRPQVSS KLQEVIQTQV PALSALSRFY ASKSFPPHTL
     ISMPALSPTM TAGNIGVWQK NAGDALQPGD VLVEIETDKA QMDFEFQDEG VLAKVLKESG
     EKDIAVGQPI AVLVEDGADV AAFESFTLAD AGGDKPAPAE QKEEPKSAEP SAPAPAEEAP
     AAQEPETSGE KLQPSIDREP SISPAAKVLA LEKGVSIKGL KGTGRGGVIT KEDVEKAKPA
     ATAVSAEASF EEIPVSSMRK TIANRLKQSM AENPHYFVST TLSVTKLLKL RQALNASAEG
     QYKLSVNDFL VKACAVALLK VPQVNSSWRE ENGQAVIRQH NTADISVAVS TPSGLITPVV
     KNVQGLGLSS ISKQIKDLGK RARENKLKPE EYQGGTFTIS NMGMNAAVER FTAVINPPQA
     GILAVGTTRK VAVPVETEEG TVTEWDDQIV VTGSFDHKVV DGAVGGEWIK ELKKVVENPL
     ELLL
//
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