ID A0A0S8EMY5_9BACT Unreviewed; 326 AA.
AC A0A0S8EMY5;
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=AMK72_04790 {ECO:0000313|EMBL:KPK49329.1};
OS Planctomycetes bacterium SM23_25.
OC Bacteria; Planctomycetota.
OX NCBI_TaxID=1704028 {ECO:0000313|EMBL:KPK49329.1, ECO:0000313|Proteomes:UP000052058};
RN [1] {ECO:0000313|EMBL:KPK49329.1, ECO:0000313|Proteomes:UP000052058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_25 {ECO:0000313|EMBL:KPK49329.1};
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:KPK49329.1}.
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DR EMBL; LJTY01000070; KPK49329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8EMY5; -.
DR PATRIC; fig|1704028.3.peg.639; -.
DR Proteomes; UP000052058; 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 326 AA; 35635 MW; A59DECD6D75090B3 CRC64;
MPEIMYREAI CDALAEEMRR DPRVFVMGED VAIYGGAYSA TKGLWEEFGD ERVRDTAISE
AAIAGAATGA AMCGMRPVAE IMYVDFMTLA MDQFVNQAGK NRYMFGGKTT VPMVIRTEGG
AGRSIAAHHS QSLEAWFCHA PGVFVVMPST PYDAKGLLKT SIRDDNPILF IEHKMLYGTK
GEVPDKEYLI PLGEAAVRRP GDDVTIIGYS LMALRAVEAG DALAEEGIHA EVIDLRCLKP
LDIDCILESV KKTGRLVLAS EGYQEANFVC EIIAKVQQFA FDYLDAPIER VCAANCPLPM
SPVLENEAVP TTEKVIAAAK RTLRRA
//
