ID   A0A0S9Q0X2_9ACTN        Unreviewed;       327 AA.
AC   A0A0S9Q0X2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=2-oxoisovalerate dehydrogenase {ECO:0000313|EMBL:KQP63541.1};
GN   ORFNames=ASF47_15930 {ECO:0000313|EMBL:KQP63541.1};
OS   Nocardioides sp. Leaf285.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736322 {ECO:0000313|EMBL:KQP63541.1, ECO:0000313|Proteomes:UP000051495};
RN   [1] {ECO:0000313|EMBL:KQP63541.1, ECO:0000313|Proteomes:UP000051495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf285 {ECO:0000313|EMBL:KQP63541.1,
RC   ECO:0000313|Proteomes:UP000051495};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP63541.1, ECO:0000313|Proteomes:UP000051495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf285 {ECO:0000313|EMBL:KQP63541.1,
RC   ECO:0000313|Proteomes:UP000051495};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KQP63541.1}.
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DR   EMBL; LMNH01000004; KQP63541.1; -; Genomic_DNA.
DR   RefSeq; WP_056864974.1; NZ_LMNH01000004.1.
DR   AlphaFoldDB; A0A0S9Q0X2; -.
DR   Proteomes; UP000051495; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000051495}.
FT   DOMAIN          6..181
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   327 AA;  35699 MW;  98643B338BF23A65 CRC64;
     MSTHKVTLAK SLNMGLRRAM EDDPKVLLMG EDVGKLGGVF RITDGLQKDF GEDRVIDSPL
     AESGIVGTAV GMALRGYRPV VEIQFDGFVY PAYDQIVCQV AKMSYRSKGR SRMPMVIRIP
     YGGGIGAVEH HSESPEAQFA HTPGLKVVTC SNPVDGYWMI QQAIASDDPV VFLEPKRQYH
     ADKADLDTTA TPAPLFTSRV VRRGTDVTLL AYGPMVKTAM KAAEAAATEG RSLEVIDLRT
     LSPLDMAPVL ESVRRTGRAV VAHEAHVNLG LGAELSARIT EQCFYSLEAP VLRVGGFDTP
     YPASRIEEDF LPDLDRVLDA VDRSMEF
//