ID A0A0A1MY49_9BACI Unreviewed; 325 AA.
AC A0A0A1MY49;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281};
GN Name=pdhB {ECO:0000313|EMBL:CEI84444.1};
GN ORFNames=BN997_04393 {ECO:0000313|EMBL:CEI84444.1};
OS Oceanobacillus oncorhynchi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI84444.1, ECO:0000313|Proteomes:UP000040453};
RN [1] {ECO:0000313|EMBL:CEI84444.1, ECO:0000313|Proteomes:UP000040453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oc5 {ECO:0000313|EMBL:CEI84444.1,
RC ECO:0000313|Proteomes:UP000040453};
RA Urmite Genomes Urmite Genomes;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|ARBA:ARBA00025211}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
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DR EMBL; CDGG01000001; CEI84444.1; -; Genomic_DNA.
DR RefSeq; WP_042535270.1; NZ_JABUYK010000004.1.
DR AlphaFoldDB; A0A0A1MY49; -.
DR STRING; 545501.BN997_04393; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000040453; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1.
DR PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 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:CEI84444.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000040453}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 325 AA; 35810 MW; 467089B41D82019E CRC64;
MAQMTMIQAI TDAMRVELKN DENVLVFGED VGQNGGVFRA TEGLQDEFGE DRVFDTPLAE
SGIGGLAIGL AMEGFRPVPE IQFFGFVYEV MDSINGQMAR LRYRSGGHYN APITVRAPFG
GGVHTPELHA DSLEGLIAQQ PGMKVVIPST PYEAKGLLIS AIRDNDPVVF LEHMKLYRSF
RGEVPEEDYT VELGKADVKR EGTDVTLLAY GAMVHSSLKA AEELEKDGIS AEVIDLRTVS
PVDYDTILES VKKTNRVVFV QEAQRQAGIA GQVISEVQER AILHLEAPIL RVTAPDTVYA
FSDAEEVWLP DHKDIVERVN EVINF
//
