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Database: UniProt
Entry: A0A399EUS7_9DEIN
LinkDB: A0A399EUS7_9DEIN
Original site: A0A399EUS7_9DEIN 
ID   A0A399EUS7_9DEIN        Unreviewed;       332 AA.
AC   A0A399EUS7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 10.
DE   SubName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000313|EMBL:RIH86839.1};
DE            EC=1.2.4.1 {ECO:0000313|EMBL:RIH86839.1};
GN   Name=pdhB {ECO:0000313|EMBL:RIH86839.1};
GN   ORFNames=Mlute_01156 {ECO:0000313|EMBL:RIH86839.1};
OS   Meiothermus luteus.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX   NCBI_TaxID=2026184 {ECO:0000313|EMBL:RIH86839.1, ECO:0000313|Proteomes:UP000265800};
RN   [1] {ECO:0000313|EMBL:RIH86839.1, ECO:0000313|Proteomes:UP000265800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 52599 {ECO:0000313|EMBL:RIH86839.1,
RC   ECO:0000313|Proteomes:UP000265800};
RA   Da Costa M.S., Albuquerque L., Raposo P., Froufe H.J.C., Barroso C.S.,
RA   Egas C.;
RT   "Meiothermus luteus KCTC 52599 genome sequencing project.";
RL   Submitted (AUG-2018) 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:RIH86839.1}.
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DR   EMBL; QWKZ01000028; RIH86839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A399EUS7; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000265800; Unassembled WGS sequence.
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:RIH86839.1};
KW   Pyruvate {ECO:0000313|EMBL:RIH86839.1}.
FT   DOMAIN          10..185
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   332 AA;  36102 MW;  641D12FD52833B7F CRC64;
     MIAERQTRVL NNVQAINEAL DLALERDPRV VVFGEDVGTM GGVFRASDGL QQKYGEQRVF
     DTPLAESGIV GFGIGLAMAG LRPVAEIQFA GFLYPALDQI LSHLGRMRHR TRGRFSIPMV
     IRAPYGGGVK TPEQHADSPE AILAHVPGVK VVIPSSPERA KGLLLAAIED PDPVFFLEAI
     KLYRGVKAEV PEGYYTLPLG RARVVREGDA ASLFCYGGMV EVCQKAAEVA AREGVELEIV
     DLETLVPLDT ETIFASVQKT GRAVVVYEAM RTGGFGAEVA ARIAEEALDY LQAPIVRVAG
     WDAPYPPFSA VENYYRPDAK RVLEAVRKVL TH
//
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