ID A0A1I2ACW3_9BACI Unreviewed; 343 AA.
AC A0A1I2ACW3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=Pyruvate dehydrogenase E1 component beta subunit {ECO:0000313|EMBL:SFE41801.1};
GN ORFNames=SAMN05192532_101794 {ECO:0000313|EMBL:SFE41801.1};
OS Alteribacillus iranensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacillus.
OX NCBI_TaxID=930128 {ECO:0000313|EMBL:SFE41801.1, ECO:0000313|Proteomes:UP000199516};
RN [1] {ECO:0000313|EMBL:SFE41801.1, ECO:0000313|Proteomes:UP000199516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23995 {ECO:0000313|EMBL:SFE41801.1,
RC ECO:0000313|Proteomes:UP000199516};
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FONT01000001; SFE41801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2ACW3; -.
DR STRING; 930128.SAMN05192532_101794; -.
DR Proteomes; UP000199516; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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:SFE41801.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199516}.
FT DOMAIN 22..197
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 343 AA; 37878 MW; DF73F87933C263F8 CRC64;
MSLISANKKN KTNDFALGQK NITMVQAITD ALDVMLERDE RVMLLGEDIG KNGGVFRATD
GLQKKYGEDR VVDTPLSEAG IIGTGVGLAV NGMRPVLEIQ FLGFIYPAFE QIATHVTRMR
MRTRGELTVP MVIRAPYGAG VRAPEIHSDS TEAYFTHMPG IKVICPSSPY DAKGLLISAM
EDPDPVLFME SMRLYRSGKE EVPEGYYKEE IGKGKKVKEG KDVTVITWGA MVKTAKEAAD
SMENRDIECD VIDVRTLYPL DQDIIADSVQ KTGRVVIVHE AHETGGVGND ILSVINKQAF
MYLKAPIEKV TGFDVPVPMF SLEDHYLPSA ARIQTAIHKV YSF
//