ID A0A1Y4SFF2_9FIRM Unreviewed; 826 AA.
AC A0A1Y4SFF2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-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=B5E77_02285 {ECO:0000313|EMBL:OUQ28606.1};
OS Lachnoclostridium sp. An131.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965555 {ECO:0000313|EMBL:OUQ28606.1, ECO:0000313|Proteomes:UP000199743};
RN [1] {ECO:0000313|Proteomes:UP000199743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An131 {ECO:0000313|Proteomes:UP000199743};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
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}.
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:OUQ28606.1}.
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DR EMBL; NFLI01000002; OUQ28606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4SFF2; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000199743; 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 Reference proteome {ECO:0000313|Proteomes:UP000199743}.
FT DOMAIN 479..652
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 826 AA; 91903 MW; D46C7A4A1E5D2ADD CRC64;
MPKSIFVDPD KMRAEGKITF KDIPINVYKK SVQEELDEGN YTKEDLLRIF RDMTICREFE
DMLNQIKTQA KYADVETTYP GPAHLSLGQE AAAVGEAYLL GKEDFTFGSH RSHSEILAKG
LSCIQKLEDK ELLDIMENFF DGKTLKAIKT VSKAEGDVKE LAIEFLVYGA LAELFARENG
FHKGLGGSMH AFFLPFGVYP NNALVGGSAT IATGASLFKK CNDREGVVVA NLGDGSMGRG
PVWEALSFAT MDQYRTLWEE GRKGGLPLIF NINNNSYGMG GQTCGETMGY GELARMGAGV
TESQLHAERV DGYNPLAVID AYRRKLPLVK SGEGPVFLDV VTYRLLGHST SDQNAYRTKE
EIEAWKAQDP LVTYRKALVE AGVADDSVFE EIWAKTKERM ARICRLAADK EASPYLDFDK
DPAIIERVMF NNGKQRNMDP GREPSVMGPK ENCKRYRDIQ KKIRTHYMDG QEVSSMKRYN
IRDAVFEPML NKYYEDPTLI AYGEDVRDWG GAFAVYRGFT DVIPYSRLFN SPISESAIVG
TGVGYTMCGG RAVIELMYGD FIGCCGDEIF NQMAKWQAMS AGILKMPLIL RVSVGSKYGA
QHSQDWTSMC AHVPGLKVCF PATPYEAKGL MQAALNGTDP VVFFESQRIY DVGEKFHEGG
VPKEEYELPF GDVDVITTGS DITVLTIGAT LYRAYDAVQE LKEKYGLSAE LINLCSLVPL
DYTKIIESVK KTGKVVLASD ACARGSFLDE VAKNITELAF DYLDAPPAVV GAQNWITPPF
EYDKYFFPQK EWILDAINEK LVPLKGYTPV TNVTAEEQMR KLKLGV
//