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Database: UniProt
Entry: A0A0Q6PSN7_9MICO
LinkDB: A0A0Q6PSN7_9MICO
Original site: A0A0Q6PSN7_9MICO 
ID   A0A0Q6PSN7_9MICO        Unreviewed;       336 AA.
AC   A0A0Q6PSN7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=2-oxoisovalerate dehydrogenase {ECO:0000313|EMBL:KQV05123.1};
GN   ORFNames=ASC63_15115 {ECO:0000313|EMBL:KQV05123.1};
OS   Leifsonia sp. Root112D2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=1736426 {ECO:0000313|EMBL:KQV05123.1, ECO:0000313|Proteomes:UP000051914};
RN   [1] {ECO:0000313|EMBL:KQV05123.1, ECO:0000313|Proteomes:UP000051914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root112D2 {ECO:0000313|EMBL:KQV05123.1,
RC   ECO:0000313|Proteomes:UP000051914};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV05123.1, ECO:0000313|Proteomes:UP000051914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root112D2 {ECO:0000313|EMBL:KQV05123.1,
RC   ECO:0000313|Proteomes:UP000051914};
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:KQV05123.1}.
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DR   EMBL; LMCU01000002; KQV05123.1; -; Genomic_DNA.
DR   RefSeq; WP_055816223.1; NZ_LMCU01000002.1.
DR   AlphaFoldDB; A0A0Q6PSN7; -.
DR   STRING; 1736426.ASC63_15115; -.
DR   OrthoDB; 3457658at2; -.
DR   Proteomes; UP000051914; 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:UP000051914}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   336 AA;  35923 MW;  40A8FA9A705CDB1A CRC64;
     MTTLTMAKAI TAGLREALKA DEKVVLMGED IGKLGGVYRV TDGLQRDFGE RRVMDTPLAE
     SGILGAAVGL AYRGYRPVCE IQFDGFIYPA FDQIVSQVAR MRGRTQGRVS MPLTIRVPFG
     GGIGSAEHHS DSPEAYFAHA AGLRVVSVST AQDAFTMIRQ AIASDDPVLY FEPKRRYHVK
     GEVDEAAPLS EALPMGRARI VMPGTDATLV TYGPLVGTAC DAAVAASDEG ISIEVIDLRS
     LSPIDFETVE ASVRKTGRLV VTHEAALSGG LGAEVAASIT ERCFAELRHA PVRVTGFDVP
     YPVAKLESHY LPDLDRILDG VDRALGRPHS LTGVVA
//
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