ID A0A1Q5P8W6_9BACT Unreviewed; 802 AA.
AC A0A1Q5P8W6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=A3841_05380 {ECO:0000313|EMBL:OKL38582.1};
OS Pontibacter flavimaris.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1797110 {ECO:0000313|EMBL:OKL38582.1, ECO:0000313|Proteomes:UP000186551};
RN [1] {ECO:0000313|EMBL:OKL38582.1, ECO:0000313|Proteomes:UP000186551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S10-8 {ECO:0000313|EMBL:OKL38582.1,
RC ECO:0000313|Proteomes:UP000186551};
RA Zhang G., Zhang R.;
RT "Genome sequence of Pontibacter sp. nov., of the family cytophagaceae,
RT isolated from marine sediment of the Yellow Sea, China.";
RL Submitted (MAR-2016) 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:OKL38582.1}.
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DR EMBL; LVWA01000012; OKL38582.1; -; Genomic_DNA.
DR RefSeq; WP_073854503.1; NZ_LVWA01000012.1.
DR AlphaFoldDB; A0A1Q5P8W6; -.
DR STRING; 1797110.A3841_05380; -.
DR OrthoDB; 9769337at2; -.
DR Proteomes; UP000186551; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 468..642
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT COILED 324..351
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 802 AA; 89719 MW; 2D55A01CA99F7BC7 CRC64;
MQTAEASITQ RLTSEEILHD YRIAWESRQA SLTGRKEVFM GKAKFGIFGD GKEVAQLAMA
KFFRNGDFRS GYYRDQTFMF AVGELTLQQY FAQLYAHTDV EAEPSTAGRA MNGHFGTRSL
NEDGQWKNLM EQKNSSADIS PTAAQMPRLL GLAYASKLYR QNPALQSMSD FSVNGNEVAF
GTIGNASTSE GMFFEAINAA GVLQVPMLVS VWDDAYGISV PAEYQTTKGS ISEILAGFQR
NAEGEQGYEI FKVKGWDYAA LCDTYEAAVR VCREQHVPVL VHVEELTQPQ GHSTSGSHER
YKSKERLEWE AEYDCLKKMR EWILESEIAS VEQLEQLEAE AKDAVKVARS NAWNDFAEDI
KVDHEEALRL LDGLAEASEH ITEIATITEE LRKTLNPIRS DAVRAVRKAL RYVRDEHNMA
KRELVGWLEQ TLGENADRYN SYLYSQSEEA ALLVEEVKPE FDESSPVVDG REVLQACFDA
ILSRDPRVFA IGEDVGFIGD VNQAFAGLQE KHGELRVTDT GIRECTIIGQ GIGAALRGLR
PITEIQYLDY LLYAIQILSD DVACLQYRTK GGQKAPLIVR TRGHRLEGIW HSGSPIGMIL
NSIRGMHVLV PRNMTQAAGF YNTLLKSDEP ALVIECLNGY RLKERIPNNI GEFTVPLGKP
EVLKEGADIT IVTYGSMCRI VMEAARQLEE FGISAEVIDV QSLLPFDVDH VVTDSIRKTN
RVLFTDEDVP GGASAYMMQQ VVDEQGAWRW LDSKPQCLSA QAHRPPYGSD GDYFSKPNTE
DVFEAVYEIL HEADPKAFPS IY
//
