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Database: UniProt
Entry: A0A1I4RI27_9ACTN
LinkDB: A0A1I4RI27_9ACTN
Original site: A0A1I4RI27_9ACTN 
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
//
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