ID A0A101FX16_9CHLR Unreviewed; 326 AA.
AC A0A101FX16;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=XD73_1146 {ECO:0000313|EMBL:KUK45979.1};
OS Anaerolinea thermophila.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Anaerolinea.
OX NCBI_TaxID=167964 {ECO:0000313|EMBL:KUK45979.1, ECO:0000313|Proteomes:UP000064249};
RN [1] {ECO:0000313|EMBL:KUK45979.1, ECO:0000313|Proteomes:UP000064249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=46_16 {ECO:0000313|EMBL:KUK45979.1};
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 -!- 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:KUK45979.1}.
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DR EMBL; LGFU01000099; KUK45979.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101FX16; -.
DR PATRIC; fig|167964.4.peg.1149; -.
DR Proteomes; UP000064249; 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;
KW Pyruvate {ECO:0000313|EMBL:KUK45979.1}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 326 AA; 35704 MW; 7254B1AF9115D9AD CRC64;
MSRMTVREAI SKALWEEMER DESVFIQGEE VGVWGGTYAV TKGFLDHFGE KRVRDTPIAE
TAIVGSAIGA ALTGLRPVAE LMTINFAFVA MDHIINQAAK LHYMFGGQFK LPLVIRATSG
GGRQLGATHS QTPDAIFAHF PGLVVVSPGT PADAKGLLKS AIRSDDPVLF IENATLYQTR
GEVPDDKDYL EPLGKSKVQR KGDDVTIVAY SKMVQSALEA AEMLSEDGIE AEVVDLRSLR
PLDMDPVIES FKRTNRAVVV EEGWRSYGVG SEVASRIYEL AFDYVDAPVK RVAQAEVPLP
YNAKLEQLAL PQTEDIYHAA KEVLYG
//
