ID A0A218W9F9_PUNGR Unreviewed; 389 AA.
AC A0A218W9F9;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) {ECO:0000256|ARBA:ARBA00012277};
DE EC=1.2.4.4 {ECO:0000256|ARBA:ARBA00012277};
GN ORFNames=CDL15_Pgr025483 {ECO:0000313|EMBL:OWM69296.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM69296.1, ECO:0000313|Proteomes:UP000197138};
RN [1] {ECO:0000313|Proteomes:UP000197138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX PubMed=28654223; DOI=10.1111/tpj.13625;
RA Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT "The pomegranate (Punica granatum L.) genome and the genomics of
RT punicalagin biosynthesis.";
RL Plant J. 91:1108-1128(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] = CO2 +
CC N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase];
CC Xref=Rhea:RHEA:13457, Rhea:RHEA-COMP:10488, Rhea:RHEA-COMP:10489,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:83099, ChEBI:CHEBI:83142; EC=1.2.4.4;
CC Evidence={ECO:0000256|ARBA:ARBA00043720};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13458;
CC Evidence={ECO:0000256|ARBA:ARBA00043720};
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:OWM69296.1}.
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DR EMBL; MTKT01004939; OWM69296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218W9F9; -.
DR Proteomes; UP000197138; 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 39..244
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 389 AA; 42529 MW; BB2776323E3B3947 CRC64;
MASALRRLGS AAARRGLSTA CEDTKKSLFQ LPQAGGKSSN LCSAINQALH IALESDPRYR
LVLSEMSPII PKPNISLLPS LHATDNRHSY LFGEDVSFGG VFRCTTGLAD RYGKSRVFNT
PLCEQGIVGF GIGLAAMGNR AIAEIQFADY IFPAFDQIVN EASKFRYRSG NQFNCGGLTI
RAPYGAVGHG GHYHSQSPEA FFCHVPGIKV VIPRSPRQAK GLLLSCIRDP NPVVFFEPKW
LYRQAIEEVP EEDYMLPLSE AEVIREGSDI TVVGWGAQLS IMEQACAGAE KEGISCELID
LKTLIPWDKE TVEASVRKTG RLLISHEAPV TGGFGAEISA SIVERCFLRL EAPVARICGL
DTPFPLVFEP FYMPTKNKIL DAIKATVNY
//
