ID A0A1I4RI27_9ACTN Unreviewed; 690 AA.
AC A0A1I4RI27;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN04487980_1002129 {ECO:0000313|EMBL:SFM51875.1};
OS Streptomyces sp. cf124.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1761903 {ECO:0000313|EMBL:SFM51875.1, ECO:0000313|Proteomes:UP000198530};
RN [1] {ECO:0000313|EMBL:SFM51875.1, ECO:0000313|Proteomes:UP000198530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF124 {ECO:0000313|EMBL:SFM51875.1,
RC ECO:0000313|Proteomes:UP000198530};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FOUV01000002; SFM51875.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4RI27; -.
DR Proteomes; UP000198530; 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 CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 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 Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transferase {ECO:0000256|ARBA:ARBA00023315};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 369..544
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..359
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 690 AA; 73703 MW; E5BC717CDEBB9262 CRC64;
MADGLENLDD PDDPDDAEDP DDLDDPDDPR ITTGTPAHLD GDLDEVDAGR LLALYERMAL
IRRTEQAAHA LSLAGPVKGA THLAAGHEAV AVGASAALRP DDYVFATYRG HHHALARGAT
PEECLAELMG RATGLCRGKG GSTHLTKASV GMLGSYAVVG AHLPMAVGAA WSARLRGTDR
IAVAFFGDGA TNVGAFHEAL NLAAVWRLPV LFVCENNLYM EYTPTADVTA VPRPAADRAP
AYGLDGEVVD GNDVVLVRRA VARLADRARA GEGPGLLEAR TYRHYGHSRA DPGTYRPADE
VAHWLRHDPL DLARAPARRP RRVHPRRRRA RRADGRPGRR GGRAGTRARP RRGAHRRMGR
RRCRMADMIT YREAVAEGLA REMRRDPTVV CLGRDIAEAQ GVFRTTAGLL KEFGPQRVWD
TPISEQAVLG AAMGAAMTGT RPVVEIMFSD FLACCWDYLA NEIPKARYVT GGQVTVPLVV
RTANGGGLGL GAQHSQATEN WALTVPGLKI AAPSTPADVV GMLAAAVRSD DPVVFFEHKA
LHATQGPPAP PDHLVELGRA RVVRPGRDIT VVALAAMVPV ALEAARLLAE EGVDAEVVDL
RTLVPLDAAT VLGSLARTSR LVTVEENPYQ GGWGGTLVSI VADEGFGLLD APVRRVAGEC
VPLPCADTLE QRVVPTVGRV MGTVRDLTAY
//