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Database: UniProt
Entry: W6TL89_9SPHI
LinkDB: W6TL89_9SPHI
Original site: W6TL89_9SPHI 
ID   W6TL89_9SPHI            Unreviewed;       549 AA.
AC   W6TL89;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   05-JUN-2019, entry version 29.
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=N824_09690 {ECO:0000313|EMBL:ETZ19733.1};
OS   Pedobacter sp. V48.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=509635 {ECO:0000313|EMBL:ETZ19733.1, ECO:0000313|Proteomes:UP000019145};
RN   [1] {ECO:0000313|EMBL:ETZ19733.1, ECO:0000313|Proteomes:UP000019145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V48 {ECO:0000313|EMBL:ETZ19733.1,
RC   ECO:0000313|Proteomes:UP000019145};
RX   PubMed=24578271;
RA   Bitzer A.S., Garbeva P., Silby M.W.;
RT   "Draft Genome Sequence of Pedobacter sp. Strain V48, Isolated from a
RT   Coastal Sand Dune in the Netherlands.";
RL   Genome Announc. 2:e00094-14(2014).
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:ETZ19733.1}.
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DR   EMBL; AWRU01000033; ETZ19733.1; -; Genomic_DNA.
DR   RefSeq; WP_048907855.1; NZ_AWRU01000033.1.
DR   STRING; 509635.N824_09690; -.
DR   EnsemblBacteria; ETZ19733; ETZ19733; N824_09690.
DR   PATRIC; fig|509635.5.peg.5245; -.
DR   Proteomes; UP000019145; 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:UP000019145};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:ETZ19733.1};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:ETZ19733.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      133    208       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      261    298       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       90    123       Disordered. {ECO:0000256|MobiDB-lite:
FT                                W6TL89}.
FT   REGION      217    260       Disordered. {ECO:0000256|MobiDB-lite:
FT                                W6TL89}.
FT   COMPBIAS    101    120       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                W6TL89}.
FT   COMPBIAS    227    245       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                W6TL89}.
SQ   SEQUENCE   549 AA;  58367 MW;  F3DDF578002C7B8C CRC64;
     MAEIVRMPKM SDTMTEGVMA KWHKKVGDKV KSGDVMAEVE TDKATMDLES YWDGTVLYIG
     VEEGKAVPVD AIIAVVGKEG EDYKAALDAE GGATPAKEEP ATEKSSSDKP VEEKKEAASA
     PAVTDADLEK QGVTVVRMPL LSDTMTEGVI AEWHKKVGDK VKNDDILADV ETDKATMEVM
     GYAEGTLLHI GVEKGQAAKV NGIIAIVGPE GTDISGILSQ GDAPAKPAAD KKSDAPVEEK
     SSPVAQKEEA PVASGNTDRV KASPLAKKIA QEKGIDLSQV AGSADGGRII KKDIENFKPA
     AKAAESGAPA EKSAPVLAQY LGEEKFTEKP VSQMRKVIAK RLSESLFTAP HFYLTMVIDM
     DAAIAARTKM NEFSPVKLSF NDLVLKAVAV ALKQHPNVNS SWRGDAIRYN EHVNIGVAIA
     VEDGLLVPVV RFADGKSLSR ISAEVKDFAQ RAKAKKLQPA DWEGSTFTVS NLGMFGIDEF
     TAIINTPDSC ILAIGGISQV PVVKNGAVVP GNIMKVTLSC DHRTVDGATG AAFLQTFKAL
     MEEPVRLLV
//
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