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Database: UniProt
Entry: A0A0D6TMQ0_9FLAO
LinkDB: A0A0D6TMQ0_9FLAO
Original site: A0A0D6TMQ0_9FLAO 
ID   A0A0D6TMQ0_9FLAO        Unreviewed;       542 AA.
AC   A0A0D6TMQ0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-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=SY27_07315 {ECO:0000313|EMBL:KIX21505.1};
OS   Flavobacterium sp. 316.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1603293 {ECO:0000313|EMBL:KIX21505.1, ECO:0000313|Proteomes:UP000032747};
RN   [1] {ECO:0000313|EMBL:KIX21505.1, ECO:0000313|Proteomes:UP000032747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=316 {ECO:0000313|EMBL:KIX21505.1,
RC   ECO:0000313|Proteomes:UP000032747};
RA   Karczewska-Golec J., Kochanowska-Lyzen M., Balut M., Golec P.,
RA   Madanecki P., Markert S., Piotrowski A., Schweder T.,
RA   Szalewska-Palasz A.;
RT   "Three Bacterial Inhabitants of the Baltic Sea under Osmotic Stress: a
RT   Genomic and a Proteomic Perspective.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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 2 lipoyl cofactors covalently.
CC       {ECO:0000256|RuleBase:RU361137};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KIX21505.1}.
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DR   EMBL; JYGZ01000003; KIX21505.1; -; Genomic_DNA.
DR   RefSeq; WP_045968719.1; NZ_JYGZ01000003.1.
DR   EnsemblBacteria; KIX21505; KIX21505; SY27_07315.
DR   PATRIC; fig|1603293.4.peg.1516; -.
DR   OrthoDB; 1626282at2; -.
DR   Proteomes; UP000032747; Unassembled WGS sequence.
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; 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.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW   Complete proteome {ECO:0000313|Proteomes:UP000032747};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:KIX21505.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032747};
KW   Transferase {ECO:0000256|RuleBase:RU361137}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      118    193       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      248    285       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION      211    242       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0D6TMQ0}.
FT   COMPBIAS    214    228       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0D6TMQ0}.
SQ   SEQUENCE   542 AA;  58012 MW;  5C7A62E1A526B86F CRC64;
     MATVITMPRL SDTMTEGTVA TWLKKVGDKI NEGDILAEIE TDKATMEFES FNAGTLLHIG
     INEGETAAVD SLLAIIGKEG EDISGILAGD KISATEENTN VEEKKVETNE AVTIPEGVVV
     VTMPRLSDTM TEGTVATWLK KVGDKINEGD ILAEIETDKA TMEFESFNAG TLLYIGVQEG
     DSAPVDTILA ILGPEGTDVS NIVANYKNES GNNSAEEVKT ETKTEEKEAV VSNSNTSVSE
     TNSGGRIFAS PLAKKIAKEK GINLSQVKGS GENGRIVKLD VENFTPSSVV TKSVETEVSQ
     ATSTVANVKP FVPAGEVFQE EIKNSQMRKV IAKRLAESKF TAPHYYLTIE LDMDNAIASR
     GLINALPETK VSFNDMVVKA SAMALKKHPQ VNSQWKDDAM IINHHVNIGV AVAVEDGLVV
     PVLKFTDQMS LSQIGANVKD MAGRAKTKKI QPAEMEGSTF TISNLGMFGI QSFTSIINQP
     NSAILSVGAI VEKPVVKNGQ IVVGNTMTVT LACDHRTVDG ATGAQFLQTF KSFMENPVTM
     LA
//
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