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Database: UniProt/TrEMBL
Entry: F9YUR2_CAPCC
LinkDB: F9YUR2_CAPCC
Original site: F9YUR2_CAPCC 
ID   F9YUR2_CAPCC            Unreviewed;       531 AA.
AC   F9YUR2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   07-JUN-2017, entry version 38.
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=Ccan_09190 {ECO:0000313|EMBL:AEK23037.1};
OS   Capnocytophaga canimorsus (strain 5).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK23037.1, ECO:0000313|Proteomes:UP000008895};
RN   [1] {ECO:0000313|EMBL:AEK23037.1, ECO:0000313|Proteomes:UP000008895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5 {ECO:0000313|Proteomes:UP000008895};
RX   PubMed=21914877; DOI=10.1128/JB.05853-11;
RA   Manfredi P., Pagni M., Cornelis G.R.;
RT   "Complete genome sequence of the dog commensal and human pathogen
RT   Capnocytophaga canimorsus strain 5.";
RL   J. Bacteriol. 193:5558-5559(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: 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 2 lipoyl cofactors 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; CP002113; AEK23037.1; -; Genomic_DNA.
DR   RefSeq; WP_013997027.1; NC_015846.1.
DR   STRING; 860228.Ccan_09190; -.
DR   EnsemblBacteria; AEK23037; AEK23037; Ccan_09190.
DR   KEGG; ccm:Ccan_09190; -.
DR   eggNOG; ENOG4105C7S; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; POG091H0NG1; -.
DR   Proteomes; UP000008895; Chromosome.
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; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   TIGRFAMs; TIGR01349; PDHac_trf_mito; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:AEK23037.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008895};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00100674};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008895};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:AEK23037.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      119    194       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   531 AA;  56850 MW;  FB1E59A7A268234D CRC64;
     MAEIINMPRL SDTMEEGVVA KWLKKVGDHI QEGDILAEIE TDKATMEFES FYSGTLLHIG
     LQEGETAKVD TLLAIVGKEG EDISALIGGG SSAPKTEETK SESKTTPVPV ANVAKPEGAE
     IVTMPRLSDT MTEGTVATWL KKVGDEVSEG DILAEIETDK ATMEFESFYS GTLLYIGIEE
     GGSAPIDAVL AIIGKKGTDV DAVLAHAKGE NTPQAPKPTE NKSAEKTEAI AKETPKTSNN
     QNERIFVSPL AKKIAEEKGI NLSEVQGSGE NGRIIKKDVE NFVPSAKTSA SAPTQSASIV
     TTFGEESSDE VKNSQMRKTI AKRLSESKFT APHYYLSIEI DMENAIASRT QINNLPETKV
     SFNDLVLKAC AMALKKHPQV NTSWKGDVTV YNKHIHLGVA VAVEDGLVVP VLKFADQLSL
     SQIGGQVKDL AGKARNKKLT PAEMEGSTFT ISNLGMFGIE SFTSIINQPN SAILSVGAIV
     EKPVVKNGQI VIGNTMKLTL ACDHRTVDGA TGAQFLQTLK AFLENPVTML A
//
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