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
//