ID A0A0Q5LQR8_9MICO Unreviewed; 336 AA.
AC A0A0Q5LQR8;
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:KQR52571.1};
GN ORFNames=ASF88_13735 {ECO:0000313|EMBL:KQR52571.1};
OS Leifsonia sp. Leaf336.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736341 {ECO:0000313|EMBL:KQR52571.1, ECO:0000313|Proteomes:UP000050966};
RN [1] {ECO:0000313|EMBL:KQR52571.1, ECO:0000313|Proteomes:UP000050966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf336 {ECO:0000313|EMBL:KQR52571.1,
RC ECO:0000313|Proteomes:UP000050966};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR52571.1, ECO:0000313|Proteomes:UP000050966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf336 {ECO:0000313|EMBL:KQR52571.1,
RC ECO:0000313|Proteomes:UP000050966};
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:KQR52571.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMOZ01000002; KQR52571.1; -; Genomic_DNA.
DR RefSeq; WP_055919406.1; NZ_LMOZ01000002.1.
DR AlphaFoldDB; A0A0Q5LQR8; -.
DR STRING; 1736341.ASF88_13735; -.
DR OrthoDB; 3457658at2; -.
DR Proteomes; UP000050966; 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:UP000050966}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 336 AA; 35864 MW; 3F2A9F0C12B0405F CRC64;
MTALTMVKAI NAGLRRSLAD DDRVVLMGED IGTLGGVFRV TDGLQTEFGP RRVMDSPLAE
SGILGTAVGM AYRGLRPVVE IQFDGFVYPA FDQIVSQVAR MHYRTAGAVR MPITIRVPFA
GGIGAAEHHS DSPEAYFAHT AGLRVVSPST PQDAYTLIQQ AIASDDPVLF FEPKRRYHAK
GDVDEQAPLQ DARPMGTARV VAPGNDVTLV TYGGLVQLAT DASLAAADEG VSVEVIDLRS
LSPLDLDTVA ASVRKTGRLV VTHEAALSGG LGAEISASIT ERCFYHLEHA PVRVTGHDIP
YPAAKLEAAH LPDLDRILDG IDRAMDRPNS LSGVED
//
