ID A0A136PI82_9ACTN Unreviewed; 329 AA.
AC A0A136PI82;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=2-oxoisovalerate dehydrogenase {ECO:0000313|EMBL:KXK58108.1};
GN ORFNames=AWW66_31730 {ECO:0000313|EMBL:KXK58108.1};
OS Micromonospora rosaria.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK58108.1, ECO:0000313|Proteomes:UP000070620};
RN [1] {ECO:0000313|EMBL:KXK58108.1, ECO:0000313|Proteomes:UP000070620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 803 {ECO:0000313|EMBL:KXK58108.1,
RC ECO:0000313|Proteomes:UP000070620};
RA Yang H., He X., Zhu D.;
RT "Whole genome sequence and analysis of Micromonospora rosaria DSM 803,
RT which can produce antibacterial substance rosamicin.";
RL Submitted (JAN-2016) 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:KXK58108.1}.
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DR EMBL; LRQV01000259; KXK58108.1; -; Genomic_DNA.
DR RefSeq; WP_067374402.1; NZ_LRQV01000259.1.
DR AlphaFoldDB; A0A136PI82; -.
DR OrthoDB; 3457658at2; -.
DR Proteomes; UP000070620; 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:UP000070620}.
FT DOMAIN 6..181
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 329 AA; 35756 MW; A7EFFF2D76321423 CRC64;
MATETLTLGK ALNTGLRRAL ENDPKVVIMG EDVGKLGGVF RITDGLQKDF GDQRVIDTPL
AESGIIGTAV GLAVRGYRPV CEIQFDGFVY PAYDQIVSQV AKMHYRSRGK LNIPMVIRIP
FGGGIGAVEH HSESPEAYFA HTAGLKVVSC ANPQDAYVMI QQAIASDDPI VFLEPKRRYW
EKGPVDLDAP LAEAYPLHSA RVARAGTHAT LLAYGPMVRT CLDAATAAAE DGRELEVVDL
RTLSPLDLTA AYESVRRTGR AVVVHEAPGN LGLGAEIAAR ITEECFYSLE SPVLRVTGFD
TPYPAARVEE EYLPDLDRVL DAVDRTFGW
//
