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Database: UniProt
Entry: E4UCX6_LIBSC
LinkDB: E4UCX6_LIBSC
Original site: E4UCX6_LIBSC 
ID   E4UCX6_LIBSC            Unreviewed;       428 AA.
AC   E4UCX6;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   16-JAN-2019, entry version 48.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   OrderedLocusNames=CKC_02325 {ECO:0000313|EMBL:ADR52216.1};
OS   Liberibacter solanacearum (strain CLso-ZC1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Liberibacter.
OX   NCBI_TaxID=658172 {ECO:0000313|EMBL:ADR52216.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CLso-ZC1;
RA   Lin H., Doddapaneni H.V., Lou B., Civerolo E.L., Chen C., Duan Y.,
RA   Zhou L., Glynn J.;
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADR52216.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLso-ZC1 {ECO:0000313|EMBL:ADR52216.1};
RX   PubMed=21552483; DOI=10.1371/journal.pone.0019135;
RA   Lin H., Lou B., Glynn J.M., Doddapaneni H., Civerolo E.L., Chen C.,
RA   Duan Y., Zhou L., Vahling C.M.;
RT   "The Complete Genome Sequence of 'Candidatus Liberibacter
RT   solanacearum', the Bacterium Associated with Potato Zebra Chip
RT   Disease.";
RL   PLoS ONE 6:E19135-E19135(2011).
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   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361137}.
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DR   EMBL; CP002371; ADR52216.1; -; Genomic_DNA.
DR   STRING; 658172.CKC_02325; -.
DR   EnsemblBacteria; ADR52216; ADR52216; CKC_02325.
DR   KEGG; lso:CKC_02325; -.
DR   eggNOG; ENOG4105C7S; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281566; -.
DR   KO; K00627; -.
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; 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   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:ADR52216.1};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:ADR52216.1}.
FT   DOMAIN        2     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      124    161       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   428 AA;  46732 MW;  78742892E37B0FB3 CRC64;
     MINTITMPSL SPTMKTGKLA KWLVKKGDKI YPGDIICEIE TDKAIMEFES VDEGVVHEIL
     TSEGTENIKV NSPILNILID CDGGAPAPIL PEKNFVEIEK ESSDPAISSF APTEKKVCGQ
     DFPASSPLAR RLAKENGIDL SSVSGSGPRG RIVKNDIEQL ILHNTGVKHA STAQSASIES
     MNSSVDDDIM RLFAPNSYEI IPHDNMRKTI ASRLQQSKQT IPHFYVSIDC NIDNLLSLRQ
     QMNLFAQSNK KENINKISVN DVILKAFSLA MLQVPEANVS WTTNALIRHK NIDISVAVSI
     PGGLVTPIVR QVNKKSISDI SLEVKQLVQR AKQRKLKPQE YQGGTTSVSN MGMFGISNFC
     AVINPPQSTI LAIGAGVQKP IFQNGAIKVV TIMNATLSAD HRSVDGAVAS KLLAKFKEYI
     ENPAWMLL
//
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