ID A0A0R2PNZ6_9MICO Unreviewed; 729 AA.
AC A0A0R2PNZ6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945};
GN ORFNames=ABR66_02555 {ECO:0000313|EMBL:KRO39654.1};
OS Microbacteriaceae bacterium BACL25 MAG-120322-bin65.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae.
OX NCBI_TaxID=1655574 {ECO:0000313|EMBL:KRO39654.1, ECO:0000313|Proteomes:UP000053725};
RN [1] {ECO:0000313|EMBL:KRO39654.1, ECO:0000313|Proteomes:UP000053725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL25 MAG-120322-bin65 {ECO:0000313|EMBL:KRO39654.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase
CC complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-
CC succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-
CC COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83120; EC=2.3.1.61;
CC Evidence={ECO:0000256|ARBA:ARBA00043693};
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:KRO39654.1}.
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DR EMBL; LIAY01000017; KRO39654.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2PNZ6; -.
DR Proteomes; UP000053725; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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 402..578
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 729 AA; 78699 MW; 9B74AC18095FBECC CRC64;
MSKETPLKPL EPWVKVSTTK SDWEEADPAL LATMLGQLHL IRAFEETVLE LAGEGLVHGP
AHSSVGQEGG AVGSGLSLRP TDAVNGSHRG HHQFLAKALG YVAPSGLDLK NLVTKDIQTV
VQRTMAEILG LAQGFCKGRG GSMHLQWHEA GALGTNAIVG GGVPLAAGNA FAQQRSGTTD
MTVTYFGDGA VNIGSVLESM NLTAAWDIPL IFFIENNLYA VSTTVEEATR ESRLSGRGVG
FGIPSFRVDG MDPLAVYLTM QKAEQYTREG KGPVVIEAEV YRFFHQNGAF PGSAFGYRSK
EEEESWRARD PLTLVAKQMK ALGLIDDKGV KLVREQAQAA MAAAALELVE QDPAGKPGVR
RIKPDLWPEP GFVDVGVRGD LSELSAARTQ ERSDYKGELK DVRFVDAVAA VMDRNMEQDA
RIMILGEDVH RLKGGTNGAT KGLTDKYPGR VLGTPISENA FAGLGGGLAL DGRYRPVVEF
MYPDFLWVAA DQVFNQIGKA RHMFGGESAV PLVLRTKVAL GSGYGSQHLM DPAGIFATAP
GWRIMSASNP FDYIGMMNAA LACDDPVLMI EHVDLYGTTG EIPVSDLDYQ IPYGTARVVR
EGNDMTVLTY MSMVNHSSEA IDSSGIDAEL VDLRFLDRAS LDWDTVGESI RKTNNVLIVE
QGAQGTSYGG WLADEIQRRF FDYLDQPVER VTGSEASPSI SKVLERAAIA RTEEVVAGLQ
RVMNAKGGR
//
