ID V9XQ68_9NOCA Unreviewed; 327 AA.
AC V9XQ68;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=2-oxoisovalerate dehydrogenase subunit beta {ECO:0000313|EMBL:AHD23497.1};
GN ORFNames=Y013_24375 {ECO:0000313|EMBL:AHD23497.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD23497.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD23497.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD23497.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP006996; AHD23497.1; -; Genomic_DNA.
DR RefSeq; WP_024103677.1; NC_023150.1.
DR AlphaFoldDB; V9XQ68; -.
DR GeneID; 29938844; -.
DR KEGG; rpy:Y013_24375; -.
DR PATRIC; fig|1435356.3.peg.4914; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_0_11; -.
DR Proteomes; UP000018781; Chromosome.
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;
FT DOMAIN 6..181
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 327 AA; 35157 MW; 018323F0486949FE CRC64;
MTTTTMTLGG ALNAGLRRAL ERDPKVVIMG EDVGTLGGVF RITDTLQKDF GEGRVIDTPL
AESGIVGTAF GMALRGYRPV CEIQFDGFVY PAFDQIVSQV AKIHYRTAGA VVAPLTVRIP
YGGGIGAVEH HSESPEVYFT HTAGLRVVSP STPSDAYSMI QQAVALDDPV IFLEPKHRYW
ERGEIDTETA PDLPLTSARV VRSGSDATIV TFGALVATAL RAADIAEAEG HSLEVVDLRS
LSPIDFDTIE ASVRQTGRLV VVQEAPVFCG IGAEIAARTT ERCFYQLEAP VLRVGGFDIP
YPPAKLESHH RPDPDRILDA VDRALAA
//
