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Database: UniProt
Entry: A0A1I3WWH7_9PSEU
LinkDB: A0A1I3WWH7_9PSEU
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ID   A0A1I3WWH7_9PSEU        Unreviewed;       327 AA.
AC   A0A1I3WWH7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Pyruvate dehydrogenase E1 component beta subunit {ECO:0000313|EMBL:SFK11703.1};
GN   ORFNames=SAMN05421835_11413 {ECO:0000313|EMBL:SFK11703.1};
OS   Amycolatopsis sacchari.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=115433 {ECO:0000313|EMBL:SFK11703.1, ECO:0000313|Proteomes:UP000199025};
RN   [1] {ECO:0000313|EMBL:SFK11703.1, ECO:0000313|Proteomes:UP000199025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44468 {ECO:0000313|EMBL:SFK11703.1,
RC   ECO:0000313|Proteomes:UP000199025};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; FORP01000014; SFK11703.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3WWH7; -.
DR   STRING; 115433.SAMN05421835_11413; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000199025; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
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; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 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); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Pyruvate {ECO:0000313|EMBL:SFK11703.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199025}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   327 AA;  35858 MW;  887F01D0C9839832 CRC64;
     MPEYSLQQAL NLALQHACED DDRVLLFGED VGRLGGVFRV TDGLQAKFGE ERVFDTPLAE
     SAIMGMAVGL AMAGWRPVPE IQFDGFSYPA IDQIVNQVAR LHYRSRGTMP MPITLRLPSF
     GGIRAPEHHG ESLEALFAHV PGLKVVSPSS PSEGYRLLRQ AIADPDPVIF MEPKSRYWHK
     ESFEPTDATD PVGTSRVVRQ GKHATLVAWG AMVSRCLQVA ELAAEDGVEL EVLDLRWLKP
     IDTDGLAASV SRARRAVVVH EAPLTAGLGA EVATLITERC FGELKAPVQR VTGFDVPYPS
     GDLEDEYLPS IDRILTGVQT TLEYRRG
//
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