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Database: UniProt
Entry: A0A0J6R9Q9_9RHIZ
LinkDB: A0A0J6R9Q9_9RHIZ
Original site: A0A0J6R9Q9_9RHIZ 
ID   A0A0J6R9Q9_9RHIZ        Unreviewed;       485 AA.
AC   A0A0J6R9Q9;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   22-NOV-2017, entry version 16.
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=QR78_15625 {ECO:0000313|EMBL:KMO18223.1};
OS   Methylobacterium indicum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=1775910 {ECO:0000313|EMBL:KMO18223.1, ECO:0000313|Proteomes:UP000036498};
RN   [1] {ECO:0000313|EMBL:KMO18223.1, ECO:0000313|Proteomes:UP000036498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE2.11 {ECO:0000313|EMBL:KMO18223.1,
RC   ECO:0000313|Proteomes:UP000036498};
RA   Chaudhry V., Patil P.B.;
RT   "Comparative genomics of Methylobacterium species.";
RL   Submitted (NOV-2014) 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};
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:KMO18223.1}.
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DR   EMBL; JTHF01000126; KMO18223.1; -; Genomic_DNA.
DR   EnsemblBacteria; KMO18223; KMO18223; QR78_15625.
DR   PATRIC; fig|427683.4.peg.3176; -.
DR   Proteomes; UP000036498; 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:UP000036498};
KW   Glycolysis {ECO:0000256|RuleBase:RU364074};
KW   Lipoyl {ECO:0000256|SAAS:SAAS00100674};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364074,
KW   ECO:0000313|EMBL:KMO18223.1};
KW   Pyruvate {ECO:0000256|RuleBase:RU364074, ECO:0000313|EMBL:KMO18223.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036498};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU364074}.
FT   DOMAIN        2     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   485 AA;  51406 MW;  E3D0D70B4B052AA4 CRC64;
     MATDILMPAL SPTMEQGKLA KWLKKEGDPV KAGDILAEIE TDKATMEVEA VDEGVLAKIL
     IADGTDNVAV NTPIAVLAEE GEDPAGVEAG GGKPGGKAEA EGEAQKAPAP DMQAEGQAER
     PAPAAKTGDD KPVETPAAPA VITNRGQDPA MAEIPEGTQM VTQTVREALR DAMAEEMRRD
     DNVFVMGEEV AEYQGAYKIT QGLLQEFGAK RVVDTPITEH GFAGVGVGAA FTGLRPIVEF
     MTFNFAMQAI DQIINSAAKT LYMSGGQLGC PIVFRGPNGA AARVGAQHSH DYAAWYSNVP
     GLKVVMPYTA SDAKGLLKSA IRDPNPVVFL ENEILYGQSF PVPQLDDFTV PIGKAKVHRE
     GRDVTIVSFG IGMTYALKAA HELAEAGIEA EVIDLRTIRP MDSETVVASV KKTGRCITVE
     EGFPQSGVGA EIAARLMVDA FDYLDAPVLR ITGKDVPMPY AANLEKLALP NVAEVIEAAK
     AVCYR
//
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