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Database: UniProt
Entry: A0A239HXW0_9ACTN
LinkDB: A0A239HXW0_9ACTN
Original site: A0A239HXW0_9ACTN 
ID   A0A239HXW0_9ACTN        Unreviewed;       325 AA.
AC   A0A239HXW0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Pyruvate dehydrogenase E1 component beta subunit {ECO:0000313|EMBL:SNS86119.1};
GN   ORFNames=SAMN06893096_109101 {ECO:0000313|EMBL:SNS86119.1};
OS   Geodermatophilus pulveris.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1564159 {ECO:0000313|EMBL:SNS86119.1, ECO:0000313|Proteomes:UP000198373};
RN   [1] {ECO:0000313|EMBL:SNS86119.1, ECO:0000313|Proteomes:UP000198373}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46839 {ECO:0000313|EMBL:SNS86119.1,
RC   ECO:0000313|Proteomes:UP000198373};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; FZOO01000009; SNS86119.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239HXW0; -.
DR   OrthoDB; 3457658at2; -.
DR   Proteomes; UP000198373; 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:SNS86119.1}.
FT   DOMAIN          5..180
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   325 AA;  35201 MW;  B3EF70B853ED1BB4 CRC64;
     MTQLLTIGKA LNLGLRRAME DDAKVVLMGE DIGRLGGVFR ITDGLQKDFG EDRVVDTPLA
     EAGILGTAVG LAMRGYRPVC EIQFDGFVFP AYNQIVTQVA KIHARSRGRL AMPIVIRIPF
     GGGIGAVEHH SESPEAYFAH TPGLKVVAVS NPVDAYWGIQ QAIAHPDPVV FLEPKRRYWD
     KGEVDTDATP DPLLAARVVR AGDDVTVLAY GPMVKTALQA AEAAAEEGRS LEVVDLRAIS
     PLDLDPVVES VRRTGRCVVV HEAPVTLGLG AEIAARITES CFHSLEAPVL RVGGYDTPYP
     PSKLEEEYLP DLDRVLDAVD RAMEF
//
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