ID A0A0R2T9F7_9FLAO Unreviewed; 775 AA.
AC A0A0R2T9F7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=ABR87_01915 {ECO:0000313|EMBL:KRO83534.1};
OS Cryomorphaceae bacterium BACL7 MAG-121220-bin83.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655595 {ECO:0000313|EMBL:KRO83534.1, ECO:0000313|Proteomes:UP000051535};
RN [1] {ECO:0000313|EMBL:KRO83534.1, ECO:0000313|Proteomes:UP000051535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL29 MAG-121220-bin83 {ECO:0000313|EMBL:KRO83534.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) 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}.
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:KRO83534.1}.
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DR EMBL; LICF01000007; KRO83534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2T9F7; -.
DR Proteomes; UP000051535; Unassembled WGS sequence.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR001017; DH_E1.
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; PF00676; E1_dh; 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); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 451..625
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 775 AA; 85117 MW; EC680106F4550BBD CRC64;
MHNPDFIQSL KDDYRMAVLS RACSLLGRKE VLTGKAKFGI FGDGKEVAQL AWAKVFRDGD
FRSGYYRDQT FMMAIGALTP QQFFASLYAD TSLEREPSSG GRQMNGHFAT RSLDENGEWL
PLVDQKNVSA DISPTGGQMP RLLGLAQASK VYKALGIDNA FSRNGQEVAW GTIGNASASE
GHFWEAMNAA GVMQLPLVMC VWDDEYGISV HAKHQTLKQS ISKALAGFQR KVNKKGEEQE
PGFEIIVARG WDYPELVAAF ERAEAIARNE NVPVLLHVTE MSQPQGHSTS GSHERYKGPE
RLAWEVEYDC ITQFRAFLLE HLLISEETLL DLENSANDQA REDMKAAFAA YLEPLSVIRE
QAADCLDLLG HEQEAAQLRA DKTAMWRDSL AAVRKAATMA AALGKDVQAV QMWIETQKER
GALTYSSELH SGTALAVPVV PPVFAPDAAK VDGRVVLRDN FHALFQRYPE TLIFGEDVGA
IGDVNQGLEG MQEAFGETRV FDTGIREATI AGQGIGMAMR GLRPIAEIQY LDYLLYALEI
LSDDCATVRW RSAGGQKAPL IVRTRGHRLE GIWHSGSPMG LILGALRGMY VCVPRNMTQA
AGMYNTLLQA DEPALVIECL NGYRLKESLP TNLAEFTVPL GKVDPLREGA DITLVTYGSM
CRMVQEAADR LAALDVEVEI LDVQTLLPFD LGHTCAASVS KTNRLLVVDE DVDGGASAYL
LQKIVEDQGA FRYLDAMPST LSAKAHRPAY GSDGDYFSKP SVEDIVDKVL EIMAL
//