ID A0A0F0HKA0_9PSEU Unreviewed; 320 AA.
AC A0A0F0HKA0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=2-oxoisovalerate dehydrogenase {ECO:0000313|EMBL:KJK55999.1};
GN ORFNames=UK12_25365 {ECO:0000313|EMBL:KJK55999.1};
OS Saccharothrix sp. ST-888.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK55999.1, ECO:0000313|Proteomes:UP000033409};
RN [1] {ECO:0000313|EMBL:KJK55999.1, ECO:0000313|Proteomes:UP000033409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-888 {ECO:0000313|EMBL:KJK55999.1,
RC ECO:0000313|Proteomes:UP000033409};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-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:KJK55999.1}.
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DR EMBL; JYJF01000097; KJK55999.1; -; Genomic_DNA.
DR RefSeq; WP_045305470.1; NZ_JYJF01000097.1.
DR AlphaFoldDB; A0A0F0HKA0; -.
DR PATRIC; fig|1427391.3.peg.7878; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000033409; 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:UP000033409}.
FT DOMAIN 1..174
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 320 AA; 34414 MW; C6B57BED2011800E CRC64;
MAQALNSALR DAMRADPTVH VMGEDVGTLG GVFRITDGLT AEFGPERCLD TPLAEAGILG
TAIGMAMYGL RPVVEMQFDA FAYPALEQLF SHVAKMRNRT AGKLPLPITV RIPYGGGIGG
VEHHSDASEA YYTATPGLHV VTPATVADAY GLLRASIASD DPVVFLEPKR LYWGKQEWDP
SAPVEPIGRA VLRRTGRSAV LITYGPSLPV CLEAAEAAKA EGWDLAVLDL RSLVPFDDRT
VAEVVRSVGR AVVVHESTGF GGVGAEIAAR VTERCFHHLA APVLRVTGFD IPYPPPMLEH
HHLPGVDRIL DAVARLQWEE
//
