(data stored in SCRATCH zone)

SWISSPROT: B6HDH0_PENRW

ID   B6HDH0_PENRW            Unreviewed;       661 AA.
AC   B6HDH0;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 59.
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=Pc20g01630 {ECO:0000313|EMBL:CAP85492.1}, PCH_Pc20g01630
GN   {ECO:0000313|EMBL:CAP85492.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85492.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85492.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine
CC       = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
CC       {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; AM920435; CAP85492.1; -; Genomic_DNA.
DR   RefSeq; XP_002562722.1; XM_002562676.1.
DR   ProteinModelPortal; B6HDH0; -.
DR   STRING; 500485.XP_002562722.1; -.
DR   PRIDE; B6HDH0; -.
DR   EnsemblFungi; CAP85492; CAP85492; PCH_Pc20g01630.
DR   GeneID; 8312300; -.
DR   KEGG; pcs:Pc20g01630; -.
DR   eggNOG; KOG0557; Eukaryota.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281566; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; EOG092C32CQ; -.
DR   BioCyc; PCHR:PC20G01630-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
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; IPR004167; E3-bd.
DR   InterPro; IPR006257; LAT1.
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.
PE   3: Inferred from homology;
DR   PRODOM; B6HDH0.
DR   SWISS-2DPAGE; B6HDH0.
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transferase {ECO:0000256|RuleBase:RU361137};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    609    629       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    641    659       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       58    134       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   COILED      570    597       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   661 AA;  70775 MW;  FA355B4886B98657 CRC64;
     MVASAIRMRT PSAMFMSRGA AAMRRPQVSS KLQEVIQTQV PALSALSRFY ASKSFPPHTL
     ISMPALSPTM TAGNIGVWQK KAGDALQPGD VLVEIETDKA QMDFEFQDEG VLAKVLKESG
     EKDVSVGSPI AVLVEEGSDV SAFESFTLAD AGGDKPAPTE QKEEPKSAEP STPAPAEEAP
     AAQEPETSGE KLQPSLDREP SISPAAKVLA LEKGVSIKGL KGTGRGGVIT KEDVEKAKPA
     TTAVSGEATF EEIPVSSMRK TIANRLKQSM TENPHYFVST TLSVTKLLKL RQALNASADG
     QYKLSVNDFL VKACAVALLK VPQVNSSWRE ENGQAVIRQH KTADISVAVS TPTGLITPVV
     KNVQGLGLSS ISKQVKDLGK RARENKLKPE EYQGGTFTIS NMGMNAAVER FTAVINPPQA
     GILAVGTTRK VAIPVETEEG TVTEWDDQII VTGSFDHKVV DGAVGGEWIK ELKKVVENPL
     ELLLISPDYV LIPSRTNMSY ADAAAKGPKQ SPEDVRIQTR IFTLRRAPPV GGIYRDESES
     TASLIDVDGP HVQTVESDFL KHDVQTTTQA ERIDREAEEK EKREDEEKKK ARSQKAKSSG
     ICGNTSNPVF IANAAIATVV GAGLGFGVYK QHARGNLSWE LVGLSAGAVG IFGAVDYFVS
     K
//

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