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Database: UniProt
Entry: A0A1X7I0V5_9BACT
LinkDB: A0A1X7I0V5_9BACT
Original site: A0A1X7I0V5_9BACT 
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
//
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