ID   E8NGA6_MICTS            Unreviewed;       333 AA.
AC   E8NGA6;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, eukaryotic type, beta subunit {ECO:0000313|EMBL:BAJ76577.1};
GN   OrderedLocusNames=MTES_3613 {ECO:0000313|EMBL:BAJ76577.1};
OS   Microbacterium testaceum (strain StLB037).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ76577.1, ECO:0000313|Proteomes:UP000008975};
RN   [1] {ECO:0000313|EMBL:BAJ76577.1, ECO:0000313|Proteomes:UP000008975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StLB037 {ECO:0000313|EMBL:BAJ76577.1,
RC   ECO:0000313|Proteomes:UP000008975};
RX   PubMed=21357489; DOI=10.1128/JB.00180-11;
RA   Morohoshi T., Wang W.-Z., Someya N., Ikeda T.;
RT   "Genome sequence of Microbacterium testaceum StLB037, an N-acylhomoserine
RT   lactone-degrading bacterium isolated from potato leaves.";
RL   J. Bacteriol. 193:2072-2073(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=StLB037;
RA   Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT   "Genome sequence of Microbacterium testaceum StLB037.";
RL   Submitted (FEB-2011) 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; AP012052; BAJ76577.1; -; Genomic_DNA.
DR   RefSeq; WP_013586699.1; NC_015125.1.
DR   AlphaFoldDB; E8NGA6; -.
DR   STRING; 979556.MTES_3613; -.
DR   KEGG; mts:MTES_3613; -.
DR   eggNOG; COG0022; Bacteria.
DR   HOGENOM; CLU_012907_1_0_11; -.
DR   OrthoDB; 3457658at2; -.
DR   Proteomes; UP000008975; Chromosome.
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:BAJ76577.1}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   333 AA;  35919 MW;  ABBE58D9F3C1ABA6 CRC64;
     MTALTLGSAI NAALSKALES DDKVLLMGED IGKLGGVFRV TDGLQQRFGA QRVIDTPLAE
     AGIVGTAVGL ALRGYRPVVE IQFDGFVYPA FDQIVCQVAK LHYRSNGRIR MPLVIRIPWA
     GGVGAAEHHS ESPEAYFVHT AGLRVVAASN PQDAYVMLRQ AVASDDPVIF FEPKRLYHSK
     GEVDLDADLA DAPPMHLARV AREGTDATIV TYGAQVRTAL DAALAAEDDG LSLEVIDLRS
     LSPIDMNTVA ASVRKTGRVV VTHEAAREAG VGAELVASIT EQCFEYLEAP PQRVTGHDIP
     YPPSKLEKHH VPDLDRILFA VDRVLERGEG VLR
//