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Database: UniProt
Entry: A0A0R2T9F7_9FLAO
LinkDB: A0A0R2T9F7_9FLAO
Original site: A0A0R2T9F7_9FLAO 
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
//
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