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Database: UniProt
Entry: A0A0Q3PGC5_9BRAD
LinkDB: A0A0Q3PGC5_9BRAD
Original site: A0A0Q3PGC5_9BRAD 
ID   A0A0Q3PGC5_9BRAD        Unreviewed;       472 AA.
AC   A0A0Q3PGC5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   22-NOV-2017, entry version 15.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|RuleBase:RU364074};
DE            EC=1.2.4.1 {ECO:0000256|RuleBase:RU364074};
GN   ORFNames=ARD30_20415 {ECO:0000313|EMBL:KQK28806.1}, SAMN05660750_01286
GN   {ECO:0000313|EMBL:SKB56873.1};
OS   Bosea thiooxidans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bosea.
OX   NCBI_TaxID=53254 {ECO:0000313|EMBL:KQK28806.1, ECO:0000313|Proteomes:UP000051562};
RN   [1] {ECO:0000313|EMBL:KQK28806.1, ECO:0000313|Proteomes:UP000051562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 9174 {ECO:0000313|EMBL:KQK28806.1,
RC   ECO:0000313|Proteomes:UP000051562};
RA   Wang X.;
RT   "Draft genome of Bosea thiooxidans.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SKB56873.1, ECO:0000313|Proteomes:UP000190130}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9653 {ECO:0000313|EMBL:SKB56873.1,
RC   ECO:0000313|Proteomes:UP000190130};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO2.
CC       {ECO:0000256|RuleBase:RU364074}.
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC       {ECO:0000256|RuleBase:RU364074}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU364074};
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DR   EMBL; LMAR01000059; KQK28806.1; -; Genomic_DNA.
DR   EMBL; FUYX01000003; SKB56873.1; -; Genomic_DNA.
DR   RefSeq; WP_055729890.1; NZ_LMAR01000059.1.
DR   EnsemblBacteria; KQK28806; KQK28806; ARD30_20415.
DR   Proteomes; UP000051562; Unassembled WGS sequence.
DR   Proteomes; UP000190130; Unassembled WGS sequence.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR027110; PDHB.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR11624:SF94; PTHR11624:SF94; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000051562,
KW   ECO:0000313|Proteomes:UP000190130};
KW   Glycolysis {ECO:0000256|RuleBase:RU364074};
KW   Lipoyl {ECO:0000256|SAAS:SAAS00100674};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364074,
KW   ECO:0000313|EMBL:KQK28806.1};
KW   Pyruvate {ECO:0000256|RuleBase:RU364074, ECO:0000313|EMBL:KQK28806.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051562};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU364074}.
FT   DOMAIN        2     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   472 AA;  49656 MW;  9D9C08CFCC6DE8B7 CRC64;
     MPIDILMPAL SPTMEEGKLA KWLKKEGDQV KAGDIIAEIE TDKATMEVEA VDEGVLAKIL
     VADGTENVAV NTPIGIIAAD GEDVSKAAAA DPAKINPAVP APAAEAPKQE AAVAASADAP
     AASKPDTVPA QAKAYDASSE FPAGAEIVSM TVREALRDAM AEEMRRDKDV FVMGEEVAEY
     QGAYKVTQGL LQEFGAKRVI DTPITEHGFA GVGVGAALSG LKPIVEFMTF NFAMQAIDQI
     INSAAKTLYM SGGQMGCPIV FRGPNGAAAR VAAQHSHDYA AWYSNVPGLK VVVPYSASDA
     KGLLKSAIRD PNPVIFLENE IMYGKSFDLP KGDDFLVPIG KAKVVRPGTD VTIVSFGIGM
     NYALGAAEAL AKDGIEAEVI DLRTIRPMDI ETVVASVQKT NRCVAVEEGF PQSGVTAEIG
     MRIMEAAFDY LDAPVARVTG KDVPMPYAAN LEKLALPNIG EVVAAAKAVC YR
//
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