ID   A0A2A9CUJ7_9ACTN        Unreviewed;       326 AA.
AC   A0A2A9CUJ7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Pyruvate dehydrogenase E1 component beta subunit {ECO:0000313|EMBL:PFG18117.1};
GN   ORFNames=ATK74_2697 {ECO:0000313|EMBL:PFG18117.1};
OS   Propionicimonas paludicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Propionicimonas.
OX   NCBI_TaxID=185243 {ECO:0000313|EMBL:PFG18117.1, ECO:0000313|Proteomes:UP000226079};
RN   [1] {ECO:0000313|EMBL:PFG18117.1, ECO:0000313|Proteomes:UP000226079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15597 {ECO:0000313|EMBL:PFG18117.1,
RC   ECO:0000313|Proteomes:UP000226079};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PFG18117.1}.
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DR   EMBL; PDJC01000001; PFG18117.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A9CUJ7; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000226079; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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   Pyruvate {ECO:0000313|EMBL:PFG18117.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000226079}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   326 AA;  35250 MW;  EC2AF26A91BF3639 CRC64;
     MSTLTMAKAL NAGLRRALAG DPKVLLAGED IGRLGGVFRI TEGLQAEFGP TRVVDTPLAE
     AGIVGTAVGM ALRGYKPVVE IQFDGFVYPA FDQIVSQVSR LHFRSHGRLS VPMVVRIPYG
     GGIGAIEHHS ESPEAYFAHT PGLKVVTCAN PSDAYWMIQQ AIADPDPVIF FEPKRRYHDK
     GEVDLDASAA PDSLYQARIA RHGTDATLLT YGPMVRTCLD AAAAAEAEGR SLEVIDLRSL
     SPIDDATVFA SVRRTGRAVV VHEAVRTLGM GAELAARIQA ECFYELQAPV LRVTGYDLPY
     PPSRTEHSYL PDLDRVLDAV DQSLAH
//