ID A0A1F4APB2_9PROT Unreviewed; 326 AA.
AC A0A1F4APB2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=A3H33_12515 {ECO:0000313|EMBL:OGA13946.1};
OS Betaproteobacteria bacterium RIFCSPLOWO2_02_FULL_65_20.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1797488 {ECO:0000313|EMBL:OGA13946.1, ECO:0000313|Proteomes:UP000176396};
RN [1] {ECO:0000313|EMBL:OGA13946.1, ECO:0000313|Proteomes:UP000176396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGA13946.1}.
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DR EMBL; MEQZ01000055; OGA13946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4APB2; -.
DR Proteomes; UP000176396; 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..177
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 326 AA; 35427 MW; EF03EC8A6323471B CRC64;
MREMRYLEAM REGLREEMLR DDAVFVLGED VRNSVRGLTK GLFQEFGAKR VYDTPISEAG
FTGLATGAAI AGMRPVVEYQ INALVFVAFD QLVDQAQKLR YMMGGQGTIP VTYVVMASGA
RRGLSGQHSD HPYPLLVHMG MKTVMPATPE DAKGLMKAAI REDDPVVIFA PSALLANKGP
VPDGDYLTPL GRARIAREGK DLTIVALGPL VPDALKCAET LAAEGVSAEV IDPRSLLPLD
HDTLLRSVRK TGRVVIFDDS NRTCGYAAEI SAVVADQAWH ALRAPVRRIT RSDVPVPFSI
ALDTCVLPSP ERLLEACRAS VKETRT
//
