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Database: UniProt
Entry: A0A0S8E7L9_9BACT
LinkDB: A0A0S8E7L9_9BACT
Original site: A0A0S8E7L9_9BACT 
ID   A0A0S8E7L9_9BACT        Unreviewed;       346 AA.
AC   A0A0S8E7L9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=AMJ65_03945 {ECO:0000313|EMBL:KPK44102.1};
OS   Phycisphaerae bacterium SG8_4.
OC   Bacteria; Planctomycetota; Phycisphaerae.
OX   NCBI_TaxID=1703409 {ECO:0000313|EMBL:KPK44102.1, ECO:0000313|Proteomes:UP000051853};
RN   [1] {ECO:0000313|EMBL:KPK44102.1, ECO:0000313|Proteomes:UP000051853}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_4 {ECO:0000313|EMBL:KPK44102.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3). {ECO:0000256|ARBA:ARBA00025211}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000256|ARBA:ARBA00011870}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPK44102.1}.
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DR   EMBL; LJTR01000045; KPK44102.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8E7L9; -.
DR   PATRIC; fig|1703409.3.peg.2952; -.
DR   Proteomes; UP000051853; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
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; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1.
DR   PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   346 AA;  38405 MW;  578DAD3E7657CD6B CRC64;
     MRNISYCEAL NEAMAQEMQA DPDVFVYGID VADHKRVFGS TKGLLEKFGP DRCFSTPLSE
     DAMTGFGLGA AINGLRPIHV HMRVDFMLLA MNQLANMISS YRYMSAGRLE VPMVIRAVIG
     RGWGQAFQHS KTMHCCFAHI PGLKVVMPTT PRDAKETLVA AIRDDNPVIS IEHRWLYDVE
     DEVPEEVEPT FLGHGRVLKQ GCDITVVATS WMNIEALKAA EILAKHGVSV EVIDPVSICP
     LDEELITDSV TKTGHCIVAD NDWVYAGFGA ELAAIVSEKC FGTLKSPVAR IGFAQTPCPT
     VRHLEQEFYP NAIDIIETIE QKLDLEETDL SGEDFYSYEN KFKGPF
//
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