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Database: UniProt
Entry: A0A0Q7YQB1_9SPHN
LinkDB: A0A0Q7YQB1_9SPHN
Original site: A0A0Q7YQB1_9SPHN 
ID   A0A0Q7YQB1_9SPHN        Unreviewed;       346 AA.
AC   A0A0Q7YQB1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=2-oxoisovalerate dehydrogenase {ECO:0000313|EMBL:KQZ61692.1};
GN   ORFNames=ASD67_21120 {ECO:0000313|EMBL:KQZ61692.1};
OS   Sphingopyxis sp. Root1497.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1736474 {ECO:0000313|EMBL:KQZ61692.1, ECO:0000313|Proteomes:UP000051141};
RN   [1] {ECO:0000313|Proteomes:UP000051141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1497 {ECO:0000313|Proteomes:UP000051141};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQZ61692.1, ECO:0000313|Proteomes:UP000051141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1497 {ECO:0000313|EMBL:KQZ61692.1,
RC   ECO:0000313|Proteomes:UP000051141};
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:KQZ61692.1}.
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DR   EMBL; LMGF01000005; KQZ61692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q7YQB1; -.
DR   STRING; 1736474.ASD67_21120; -.
DR   Proteomes; UP000051141; Unassembled WGS sequence.
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;
FT   DOMAIN          13..188
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   346 AA;  37811 MW;  B3E30FD939F079AC CRC64;
     MMAPETQATT KTMNMIEAIN SAMDVMLERD PNTVVMGEDV GYFGGVFRAT AGLQKKHGKT
     RVFDTPINEC GIIGVAVGMG AYGLRPVPEI QFADYIYPGL DQLVSEAARL RYRSAADFIC
     PMTVRTPFGG GIFGGQTHSQ SPESIMTHIC GVKTVIPSNP YDAKGLLIAA IEDNDPVVFL
     EPKRIYNGPF SGYYDRPVEP WSKHEASAVP EGHYRIELGK AATVRAGEAL TILVYGTMVH
     VTKTIVEEMG IDAEIIDLRT LLPLDIGAIE ASVQKTGRCL IIHEATRTSG FGAELVALVQ
     ERCFYHLEAP VERVTGFDTP YPHSLEWAYF PGPVRIATAL TKILKD
//
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