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Database: UniProt
Entry: M4X0E7_9PSED
LinkDB: M4X0E7_9PSED
Original site: M4X0E7_9PSED 
ID   M4X0E7_9PSED            Unreviewed;       347 AA.
AC   M4X0E7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=2-oxoisovalerate dehydrogenase subunit beta {ECO:0000313|EMBL:AGI24472.1};
GN   ORFNames=H681_13010 {ECO:0000313|EMBL:AGI24472.1};
OS   Pseudomonas sp. ATCC 13867.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1294143 {ECO:0000313|EMBL:AGI24472.1, ECO:0000313|Proteomes:UP000012082};
RN   [1] {ECO:0000313|EMBL:AGI24472.1, ECO:0000313|Proteomes:UP000012082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13867 {ECO:0000313|EMBL:AGI24472.1,
RC   ECO:0000313|Proteomes:UP000012082};
RX   PubMed=23723394;
RA   Ainala S.K., Somasundar A., Park S.;
RT   "Complete genome sequence of Pseudomonas denitrificans ATCC 13867.";
RL   Genome Announc. 1:E00257-E00213(2013).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP004143; AGI24472.1; -; Genomic_DNA.
DR   AlphaFoldDB; M4X0E7; -.
DR   STRING; 1294143.H681_13010; -.
DR   KEGG; pdr:H681_13010; -.
DR   PATRIC; fig|1294143.3.peg.2622; -.
DR   eggNOG; COG0022; Bacteria.
DR   HOGENOM; CLU_012907_1_0_6; -.
DR   Proteomes; UP000012082; Chromosome.
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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          14..189
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   347 AA;  38135 MW;  2547D823AA3479E6 CRC64;
     MNPQHENAQA VTSMTMIQAL RSAMDVMLER DDNVVVFGQD VGYFGGVFRC TEGLQKKYGT
     SRVFDAPISE SGIIGAAVGM CAYGLRPVVE IQFADYVYPA TDQLVSEAAR IRYRSVGDFV
     VPMVVRMPCG GGIYGGQTHS QSPEAMFTQV CGLRTVMPSN PYDAKGLLIA CIENDDPVIF
     LEPKRLYNGP FDGHHDRPVT PWSKHPASQV PEGYYSVPLD KAVIARPGSE LTVLTYGTTV
     YVAQTAAEET GVDAEIIDLR SLWPLDLDTI VESVKKTGRC VIVHEATRTC GYGAELMSLV
     QENCFHHLES PIVRVTGWDT PYPHAQEWDY FPGPARVGAA FKRAMEV
//
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