ID W6JW47_9MICO Unreviewed; 324 AA.
AC W6JW47;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000313|EMBL:CCH72825.1};
DE EC=1.2.4.1 {ECO:0000313|EMBL:CCH72825.1};
GN Name=pdhB {ECO:0000313|EMBL:CCH72825.1};
GN ORFNames=BN11_20028 {ECO:0000313|EMBL:CCH72825.1};
OS Tetrasphaera australiensis Ben110.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1193182 {ECO:0000313|EMBL:CCH72825.1, ECO:0000313|Proteomes:UP000035763};
RN [1] {ECO:0000313|EMBL:CCH72825.1, ECO:0000313|Proteomes:UP000035763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ben110 {ECO:0000313|EMBL:CCH72825.1,
RC ECO:0000313|Proteomes:UP000035763};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:CCH72825.1}.
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DR EMBL; CAJA01000112; CCH72825.1; -; Genomic_DNA.
DR RefSeq; WP_048693017.1; NZ_HG764815.1.
DR AlphaFoldDB; W6JW47; -.
DR STRING; 1193182.BN11_20028; -.
DR OrthoDB; 3457658at2; -.
DR Proteomes; UP000035763; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 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:CCH72825.1};
KW Pyruvate {ECO:0000313|EMBL:CCH72825.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035763}.
FT DOMAIN 5..180
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 324 AA; 35492 MW; D96600F59CFB8FCA CRC64;
MSTQMTMAKA LNAGLRAAMD KDPKVVLMGE DIGKLGGVFR ITEGLQKDFG EDRVIDTPLA
EAGIVATAIG LTLRGYRPVV EIQFDGFVYP AFDHIVSQVA KLHARSLGHV KLPMVIRIPV
GGGIGAVEHH SESNEAYFAH TAGLRVISCS NPSDAYWMIQ EAIEFPDPII FYEPKRRYWD
KGEIAEAPER DLFSANVIRP GTDVTILAYG PMVRSCLQAA QAAEEEGYSL EVIDLRSLSP
LDTDAVFGSV RKTGRCVVVH EAPTFLGMGA ELAAQIQQEC FYSLEAPVLR VGGYNVPYPP
SRLEEDFLPD LDRVLDAVDR VMAH
//
