ID A0A117LTJ0_9BACT Unreviewed; 818 AA.
AC A0A117LTJ0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=XD85_0025 {ECO:0000313|EMBL:KUK66730.1};
OS Parcubacteria bacterium 34_609.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1641386 {ECO:0000313|EMBL:KUK66730.1, ECO:0000313|Proteomes:UP000053435};
RN [1] {ECO:0000313|Proteomes:UP000053435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(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 -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KUK66730.1}.
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DR EMBL; LGGG01000001; KUK66730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117LTJ0; -.
DR PATRIC; fig|1641386.4.peg.416; -.
DR Proteomes; UP000053435; Unassembled WGS sequence.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR001017; DH_E1.
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; PF00676; E1_dh; 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); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:KUK66730.1}.
FT DOMAIN 471..644
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 818 AA; 90935 MW; 4355D6E46A9F3617 CRC64;
MPKSIFIDPK EIRKSQILKI NDIPINQYKP DIKKEIKKYG EEKLLKIYYD MLVIREFESM
LNSIKTQGSY EGIEYDHKGP AHLSIGQEAA AVGQCLPLAI EDFIFGSHRS HGEVLAKCFS
AIDELGENEL LKIMKSYMDG ACLKVVEKEH KGNIKSLAQD FVLYGVLAEI FGRANGFNKG
LGGSMHVFFA PFGSMPNNAI VGGAADISVG AALFKRINQK PGMVVCNIGD GSMGCGPVWE
AMMLAAMDQY RTLWDKDIGG APPILFNFFN NFYGMGGQTS GETMGYKILA RVGAGVNPEN
LHAERVDGYN PLAVADAIER KKKILLQGNG PVLLDTITYR ISGHSPSDAS SYRTKEEIAA
WQETDCIKGY EDYLKKNRII TSNKVEALKQ EVTLRITKAL KLAASLEISP RVNPDFIETV
MFSNQYKDKM EQRTPEVLIP KNDNPRIKSL ARKSRFALDA NGKSLPKTKV FTYRDALFEA
MLHRFYEDPT MVAYGEENRD WGGAFAVYRG LTEALPYHRL FNTPISEGAI IGSGVGYALS
GGRAVVELMY SDFIGRAGDE LFNQVSKWQS MSAGLLTMPL TIRVSVGNKY GAQHSQDWTS
LLTHIPGLKV MFPATPYDAK GMLDLALRGT DPVVFFESQR LYDIGELFVS TGVPEGYYQV
PEGEPIIRKE GNDITILTVG AALYKGMEAA EELEKKYKVS AEVIDLRFIN PLNYDLIIDS
VKKTGKLVLV SDACERGSFL HTIASNITQF VFDYLDGPAV VVGSRNWITP AAEMESVFFP
QKEWIIDAIH ERLYPLDGHQ ITTDQSTTEQ IRRNKIGV
//
