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Database: UniProt
Entry: B2GFW8_KOCRD
LinkDB: B2GFW8_KOCRD
Original site: B2GFW8_KOCRD 
ID   B2GFW8_KOCRD            Unreviewed;       324 AA.
AC   B2GFW8;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Branched-chain alpha-keto acid dehydrogenase E1 beta subunit {ECO:0000313|EMBL:BAG28692.1};
DE            EC=1.2.4.4 {ECO:0000313|EMBL:BAG28692.1};
GN   OrderedLocusNames=KRH_03450 {ECO:0000313|EMBL:BAG28692.1};
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG28692.1, ECO:0000313|Proteomes:UP000008838};
RN   [1] {ECO:0000313|EMBL:BAG28692.1, ECO:0000313|Proteomes:UP000008838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC   {ECO:0000313|Proteomes:UP000008838};
RX   PubMed=18408034; DOI=10.1128/JB.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL   J. Bacteriol. 190:4139-4146(2008).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; AP009152; BAG28692.1; -; Genomic_DNA.
DR   RefSeq; WP_012397419.1; NC_010617.1.
DR   AlphaFoldDB; B2GFW8; -.
DR   STRING; 378753.KRH_03450; -.
DR   KEGG; krh:KRH_03450; -.
DR   eggNOG; COG0022; Bacteria.
DR   HOGENOM; CLU_012907_1_0_11; -.
DR   OrthoDB; 3457658at2; -.
DR   Proteomes; UP000008838; Chromosome.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
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   Oxidoreductase {ECO:0000313|EMBL:BAG28692.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008838}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   324 AA;  34970 MW;  CED7ABE24F4DA3D8 CRC64;
     MSRLTIAKAI TAGLSRAMEE DPKVVLMGED IGSLGGVYRV TEGLKDRFGA HRVLDSPLGE
     AGIVGTAVGL AQRGYRPVCE IQFDGFSFPA FNQITTQVAK IHARSEGRLT LPMTIRIPYG
     GVIGSVEHHS ESPEALYAHT AGLRIVSPSN AHDAYWMEQQ AIACNDPVII FEPKRRYWLK
     GEVDETTSPG DPFSASVIRQ GDDATVVAWG PLVPVALAAA AAAEEDGRSV EVIDLRSISP
     IDFDTLTASV RKTGRMVIAH EAPTFGGLGG EIAARVTERA FYSLEAPVLR VGAYHQPYPP
     AAVEDHYVPD LDRVLEALDR SFAY
//
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