GenomeNet

Database: UniProt
Entry: A0A127B461_9BACT
LinkDB: A0A127B461_9BACT
Original site: A0A127B461_9BACT 
ID   A0A127B461_9BACT        Unreviewed;       577 AA.
AC   A0A127B461;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   31-JUL-2019, entry version 18.
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=TH61_13380 {ECO:0000313|EMBL:AMM51975.1};
OS   Rufibacter sp. DG15C.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Rufibacter.
OX   NCBI_TaxID=1379909 {ECO:0000313|EMBL:AMM51975.1, ECO:0000313|Proteomes:UP000070672};
RN   [1] {ECO:0000313|EMBL:AMM51975.1, ECO:0000313|Proteomes:UP000070672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG15C {ECO:0000313|EMBL:AMM51975.1,
RC   ECO:0000313|Proteomes:UP000070672};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Rufibacter sp. DG15C whole genome sequencing.";
RL   Submitted (JAN-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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP010776; AMM51975.1; -; Genomic_DNA.
DR   RefSeq; WP_066510244.1; NZ_CP010776.1.
DR   EnsemblBacteria; AMM51975; AMM51975; TH61_13380.
DR   KEGG; rud:TH61_13380; -.
DR   PATRIC; fig|1379909.4.peg.2874; -.
DR   KO; K00627; -.
DR   OrthoDB; 1626282at2; -.
DR   BioCyc; GCF_001577755:G1ERD-2700-MONOMER; -.
DR   Proteomes; UP000070672; 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; 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:UP000070672};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:AMM51975.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070672};
KW   Transferase {ECO:0000256|RuleBase:RU361137}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      136    211       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      287    324       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       88    132       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      227    283       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    104    119       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    227    241       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    254    269       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   577 AA;  60061 MW;  87D4B682A020C00A CRC64;
     MAEIIRMPKM SDTMTDGVIA SWLKKVGDSV KSGDVLAEVE TDKATMELES YEDGTLLYIG
     PKNGESVPVD GVLAIIGKEG EDISGLMAEV NGGGAAPAPK AEEAPKAEAP KEEPKKEEAA
     PAPQPAAAAP TANVNAEIVR MPKMSDTMTD GTIVAWHKKV GDKVKSGDLL AEVETDKATM
     ELESYEDGTL LYIGVEAGAS VAVDGVLCII GEAGADYQAL LNGGAQSGGN ANPATAPTQE
     QATRLEEHKT EAQSQSGDGV GQASSLPTPA PAASGAAPAT GNQGRVLASP LAKKVAQEKG
     ISLTDVKGSG ENGRIVLRDV ENFTPSAAAP RTQAPVASAP ATPAAPVAAP GEAYSEVLVS
     QMRKIIAKRL AESKFSAPHF YLTMEIDMDR AMEARVSINE VSPVKVSFND LVIKAAAAAL
     RKHPAVNSSW LGDKIRYNNV INIGVAVAVE DGLLVPVVRN ADQKTLSAIS AEVKDLGGKA
     KSKKLQPSDW EGNTFTISNL GMFGIEEFTA IINPPDACIL AVGGIKQTPV VKNGQIQIGN
     IMKVTLSCDH RVVDGAVGSA FLQTLKGFLE DPVRMLV
//
DBGET integrated database retrieval system