ID A0A1X7I0V5_9BACT Unreviewed; 804 AA.
AC A0A1X7I0V5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, 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=SAMN05661096_00054 {ECO:0000313|EMBL:SMG07596.1};
OS Marivirga sericea.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Marivirgaceae; Marivirga.
OX NCBI_TaxID=1028 {ECO:0000313|EMBL:SMG07596.1, ECO:0000313|Proteomes:UP000193804};
RN [1] {ECO:0000313|EMBL:SMG07596.1, ECO:0000313|Proteomes:UP000193804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4125 {ECO:0000313|EMBL:SMG07596.1,
RC ECO:0000313|Proteomes:UP000193804};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FXAW01000001; SMG07596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7I0V5; -.
DR STRING; 1028.SAMN05661096_00054; -.
DR OrthoDB; 9769337at2; -.
DR Proteomes; UP000193804; 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};
KW Pyruvate {ECO:0000313|EMBL:SMG07596.1}.
FT DOMAIN 470..644
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 804 AA; 89833 MW; 9D76E1591DAF60BA CRC64;
MTTTKSKKDI KSKISKEEVL NDFRLGWESR HASLMGRKEV FMGKAKFGIF GDGKELAQLA
MAKSFQNGDF RSGYYRDQTF MFAIGELSIQ GYFAQLYAHT DVNADPASAG RLMNGHFATR
MLDEAGKYTK LTDSKNSSSD VSPTAAQMPR LVGLAFASKL FRENKELNKK EFEQYSINGN
EVAFGTIGNA STSEGMFYES INAAGVLQIP MLVSIWDDHY GISVPQEFHT TKGSISEVLA
GFQRSKDKKG YEILTVRGWD YEALIATYEK AAKVSREEHV PSMVHVLEMT QPQGHSTSGS
HERYKSTERL EWEAEYDCLN QFRKYIIKEK IATAEELDEI ENNAKKTAKD AKDAAWKAFI
GEIKDQQKEA LGLLNNLAEE SGKTEIAEIA AELKSAMNPL RLDNVKAVKK SLRLVINQEG
DAKDKVVNWL KAVMEEGRDR FSSHLYSESE ESALKVEVIG AKYSNDPKKV DGREVLQACF
DAALDRDPRV FAFGEDVGKI GDVNQAFAGL QDKYGDVRVM DTGIRECTII GQGIGAALRG
LRPIAEIQYL DYLLYAIQIL SDDLASLHYR TKGGQKAPLI IRTRGHRLEG VWHSGSPMGM
ILNSIRGIYV LVPRNMTQAA GFYNTMLQSD DPALIIECLN GYRLKESLPE NVGEFTVPLG
QVETIREGSD VTIVTYGSMC RVVIDAANNL ADHGISCEII DVQSLLPFDL DYQIVESIKK
TNRVIFADED VPGGATGFMM QKVLEEQKAY RFLDAQPATI TSNEHRPAYA SDGDYFSKPQ
TEDVFERVYA MMHEFDPEQY PALY
//