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Database: UniProt/TrEMBL
Entry: A0A1A7VVG6_PLAKH B3L1W6_PLAKH
LinkDB: A0A1A7VVG6_PLAKH B3L1W6_PLAKH
Original site: A0A1A7VVG6_PLAKH B3L1W6_PLAKH 
ID   A0A1A7VVG6_PLAKH        Unreviewed;       630 AA.
AC   A0A1A7VVG6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-SEP-2017, entry version 5.
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=PKNA1_C2_0605000 {ECO:0000313|EMBL:SBO23837.1},
GN   PKNA1_H1_0605000 {ECO:0000313|EMBL:SBO25623.1};
OS   Plasmodium knowlesi (strain H).
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=5851 {ECO:0000313|EMBL:SBO25623.1, ECO:0000313|Proteomes:UP000182142};
RN   [1] {ECO:0000313|EMBL:SBO25623.1, ECO:0000313|Proteomes:UP000182128, ECO:0000313|Proteomes:UP000182142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H {ECO:0000313|Proteomes:UP000182128,
RC   ECO:0000313|Proteomes:UP000182142};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003423}.
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DR   EMBL; CWHQ02000009; SBO23837.1; -; Genomic_DNA.
DR   EMBL; CWHR02000008; SBO25623.1; -; Genomic_DNA.
DR   RefSeq; XP_002261722.1; XM_002261686.1.
DR   GeneID; 7319731; -.
DR   KEGG; pkn:PKH_060480; -.
DR   KO; K00627; -.
DR   Proteomes; UP000182128; Unassembled WGS sequence.
DR   Proteomes; UP000182142; Unassembled WGS sequence.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P: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; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Complete proteome {ECO:0000313|Proteomes:UP000182128,
KW   ECO:0000313|Proteomes:UP000182142};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:SBO25623.1}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    630       Dihydrolipoamide acetyltransferase
FT                                component of pyruvate dehydrogenase
FT                                complex. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5010936703.
FT   DOMAIN       52    127       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      183    258       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   630 AA;  70976 MW;  94925A468965C3A1 CRC64;
     MILHWLSFLL CLRIYICISL PNKHGFISTL NHARASLLQS KGKNRRGVIF SQIEIKMPAL
     SSTMTSGKII KWNKDIGEYI NLGDIIMTVE SDKADMDVEA FDEGFLRVKH MGDGSEAKVG
     DTLGILTTEK DEQIEARGDD SPTGITQQSS RKEQIDVVTQ GNDTTETDTD STTTQTTQEI
     RGEEKIYVPF VSSKRNKMRI IKWTRKENDY VNKDEILFHV EDDKSTIEVE SPYYGIIKEI
     LVEEGQFADF DKPVAIISTI KAEEHPHKEQ TPLENVQLVN EENILRHYQG TLSGTKEGKL
     LLENMSSSDK QTMEERLLLN CDKYNNLSRD FFSSPRDDIP EESSKKQERD TAPPKGRDAP
     VVLPSAAEML EQNKLNPEDI KGSKIPGRIT YEDVVSHLER TGGATPAKEK IIELTKVQKA
     IKNNMLRTLS IPVFRITHFI KTNALLKLYE QVKDKISMTV LLSKCVSNVL LKHPLIYSTF
     IDEGEGKILL NEDIHIGNAL GLKSSLLTPV LKRVNKTDIY TLAAEWKKLV EKGKQGLLTL
     GEMTGSNFYI SNLGMFNTYQ FDATLPANVS CILSVGTNIA GVENFEELKI QRGMMMTLTC
     DHRHIYGSHA AAFMSDLAAF VERDIMQIFL
//
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Ontology (2)   
   GO (2)   
Gene (3)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (9)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (2)   
All databases (17)   

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ID   B3L1W6_PLAKH            Unreviewed;       630 AA.
AC   B3L1W6;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   05-JUL-2017, entry version 57.
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=PKH_060480 {ECO:0000313|EMBL:CAQ38885.1};
OS   Plasmodium knowlesi (strain H).
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=5851 {ECO:0000313|EMBL:CAQ38885.1, ECO:0000313|Proteomes:UP000031513};
RN   [1] {ECO:0000313|EMBL:CAQ38885.1, ECO:0000313|Proteomes:UP000031513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H {ECO:0000313|EMBL:CAQ38885.1,
RC   ECO:0000313|Proteomes:UP000031513};
RA   Pain A., Boehme U., Berry A.E., Mungall K., Finn R., Jackson A.P.,
RA   Mourier T., Mistry J., Pasini E.M., Aslett M., Balasubrammaniam S.,
RA   Borgwardt K., Brooks K., Carret C., Carver T.J., Cherevach I.,
RA   Chillingworth T., Clarke T.G., Galinski M.R., Hall N., Harper D.,
RA   Harris D., Hauser H., Ivens A., Janssen C.S., Keane T., Larke N.,
RA   Lapp S., Marti M., Moule S., Meyer I.M., Ormond D., Peters N.,
RA   Sanders M., Sanders S., Sergeant T.J., Simmonds M., Smith F.,
RA   Squares R., Thurston S., Tivey A.R., Walker D., White B.,
RA   Zuiderwijk E., Churcher C., Quail M.A., Cowman A.F., Turner C.M.R.,
RA   Rajandream M.A., Kocken C.H.M., Thomas A.W., Newbold C.I.,
RA   Barrell B.G., Berriman M.;
RT   "The genome of Plasmodium knowlesi strain H, a zoonotic malaria
RT   parasite with host range from monkey to man.";
RL   Nature 455:799-803(2008).
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003423}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AM910988; CAQ38885.1; -; Genomic_DNA.
DR   RefSeq; XP_002261722.1; XM_002261686.1.
DR   STRING; 5850.PKH_060480; -.
DR   EnsemblProtists; CAQ38885; CAQ38885; PKH_060480.
DR   GeneID; 7319731; -.
DR   KEGG; pkn:PKH_060480; -.
DR   EuPathDB; PlasmoDB:PKNH_0605000; -.
DR   HOGENOM; HOG000284461; -.
DR   InParanoid; B3L1W6; -.
DR   KO; K00627; -.
DR   Proteomes; UP000031513; Chromosome 6.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P: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; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031513};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031513};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:CAQ38885.1}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    630       Dihydrolipoamide acetyltransferase
FT                                component of pyruvate dehydrogenase
FT                                complex. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5010204774.
SQ   SEQUENCE   630 AA;  70976 MW;  94925A468965C3A1 CRC64;
     MILHWLSFLL CLRIYICISL PNKHGFISTL NHARASLLQS KGKNRRGVIF SQIEIKMPAL
     SSTMTSGKII KWNKDIGEYI NLGDIIMTVE SDKADMDVEA FDEGFLRVKH MGDGSEAKVG
     DTLGILTTEK DEQIEARGDD SPTGITQQSS RKEQIDVVTQ GNDTTETDTD STTTQTTQEI
     RGEEKIYVPF VSSKRNKMRI IKWTRKENDY VNKDEILFHV EDDKSTIEVE SPYYGIIKEI
     LVEEGQFADF DKPVAIISTI KAEEHPHKEQ TPLENVQLVN EENILRHYQG TLSGTKEGKL
     LLENMSSSDK QTMEERLLLN CDKYNNLSRD FFSSPRDDIP EESSKKQERD TAPPKGRDAP
     VVLPSAAEML EQNKLNPEDI KGSKIPGRIT YEDVVSHLER TGGATPAKEK IIELTKVQKA
     IKNNMLRTLS IPVFRITHFI KTNALLKLYE QVKDKISMTV LLSKCVSNVL LKHPLIYSTF
     IDEGEGKILL NEDIHIGNAL GLKSSLLTPV LKRVNKTDIY TLAAEWKKLV EKGKQGLLTL
     GEMTGSNFYI SNLGMFNTYQ FDATLPANVS CILSVGTNIA GVENFEELKI QRGMMMTLTC
     DHRHIYGSHA AAFMSDLAAF VERDIMQIFL
//
  All links  
Ontology (2)   
   GO (2)   
Gene (3)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (2)   
All databases (16)   

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