ID J8HK87_BACCE Unreviewed; 344 AA.
AC J8HK87;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Acetoin:2,6-dichlorophenolindophenol oxidoreductase subunit beta {ECO:0000313|EMBL:EJR33502.1};
GN ORFNames=IIG_02174 {ECO:0000313|EMBL:EJR33502.1};
OS Bacillus cereus VD048.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1053226 {ECO:0000313|EMBL:EJR33502.1, ECO:0000313|Proteomes:UP000006960};
RN [1] {ECO:0000313|EMBL:EJR33502.1, ECO:0000313|Proteomes:UP000006960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VD048 {ECO:0000313|EMBL:EJR33502.1,
RC ECO:0000313|Proteomes:UP000006960};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus cereus VD048.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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:EJR33502.1}.
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DR EMBL; AHEU01000012; EJR33502.1; -; Genomic_DNA.
DR RefSeq; WP_000198897.1; NZ_JH792310.1.
DR AlphaFoldDB; J8HK87; -.
DR GeneID; 56652513; -.
DR PATRIC; fig|1053226.3.peg.2201; -.
DR HOGENOM; CLU_012907_1_0_9; -.
DR Proteomes; UP000006960; 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; PTHR43257:SF3; ACETOIN:2,6-DICHLOROPHENOLINDOPHENOL OXIDOREDUCTASE SUBUNIT BETA; 1.
DR PANTHER; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 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;
FT DOMAIN 5..192
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 344 AA; 36979 MW; 641712F5A6BD2D70 CRC64;
MTRTVSMSTA INEAMKISMR RDENVILIGE DVAGGAQVDH LQDDEAWGGV LGVTKGLVQE
FGRNRILDTP ISEAGYMGAA MAAAATGLRP IAELMFNDFI GSCLDQVLNQ GAKFRYMFGG
KAKVPVTVRT MHGAGFSAAA QHSQSLYALF TSIPGIKVVV PSTPYDAKGL LLAAIEDDDP
VIFFEDKTLY NMKGEVPEGY YTIPLGKADI KREGSDVTIV AIGKQVHTAL AAAKQLSKKG
LEVEVIDPRS LSPLDEDTIL ASVEKTNRLI VIDEANPRCS IATDIAAIVA DKGFDLLDAP
IKRITAPHTP VPFSPPLEKL YLPTPEKVIE TVSEMIGDQS LLHV
//