ID D8PJF2_9BACT Unreviewed; 324 AA.
AC D8PJF2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN Name=pdhB {ECO:0000313|EMBL:CBK43526.1};
GN ORFNames=NIDE3853 {ECO:0000313|EMBL:CBK43526.1};
OS Nitrospira defluvii.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=330214 {ECO:0000313|EMBL:CBK43526.1, ECO:0000313|Proteomes:UP000001660};
RN [1] {ECO:0000313|EMBL:CBK43526.1, ECO:0000313|Proteomes:UP000001660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20624973; DOI=10.1073/pnas.1003860107;
RA Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B.,
RA Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.;
RT "A Nitrospira metagenome illuminates the physiology and evolution of
RT globally important nitrite-oxidizing bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 0:13479-13484(2010).
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}.
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DR EMBL; FP929003; CBK43526.1; -; Genomic_DNA.
DR AlphaFoldDB; D8PJF2; -.
DR STRING; 330214.NIDE3853; -.
DR KEGG; nde:NIDE3853; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_1_0; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000001660; Chromosome.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000313|EMBL:CBK43526.1};
KW Pyruvate {ECO:0000313|EMBL:CBK43526.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001660}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 324 AA; 34989 MW; 19166BFE64492E49 CRC64;
MTTITYREAV RSGLREALKR DPRVFLMGED VGKYGGTYAC SKGLLDEFGP ERIRDTPLSE
STFVGAGIGA ALGGMRPIVE VMTVNFSLLA LDQILNNAAT LRHMSGGQFN VPLVVRMATG
AGRQVAAQHS HSLEGWYAHI PGITVLTPAT VTDAQGMLLA ALQEPDPVFI FEHAYLYSME
GELEGSRPAV DISRAAVRRP GNDLSLITFG GSLWKALAAA TQLAQEGIEA EVLDLRVLRP
LDTGTILTSV RKTHRAVVID EAWRTGSFAA EIAAQIMEGA FYDLDAPVAR VCSEEVPIPY
PKHLEEAALP QPDKIVKAVR RLLG
//
