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Database: UniProt
Entry: A0A087H973_ARAAL
LinkDB: A0A087H973_ARAAL
Original site: A0A087H973_ARAAL 
ID   A0A087H973_ARAAL        Unreviewed;       357 AA.
AC   A0A087H973;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
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   OrderedLocusNames=AALP_Aa3g145900 {ECO:0000313|EMBL:KFK38675.1};
OS   Arabis alpina (Alpine rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX   NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK38675.1, ECO:0000313|Proteomes:UP000029120};
RN   [1] {ECO:0000313|Proteomes:UP000029120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX   PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA   Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA   Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA   Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA   Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA   Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA   Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA   Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA   Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT   "Genome expansion of Arabis alpina linked with retrotransposition and
RT   reduced symmetric DNA methylation.";
RL   Nat. Plants 1:14023-14023(2015).
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};
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DR   EMBL; CM002871; KFK38675.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087H973; -.
DR   EnsemblPlants; KFK38675; KFK38675; AALP_AA3G145900.
DR   Gramene; KFK38675; KFK38675; AALP_AA3G145900.
DR   eggNOG; KOG0525; Eukaryota.
DR   OMA; LPLDTCF; -.
DR   OrthoDB; 364at2759; -.
DR   Proteomes; UP000029120; Chromosome 3.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0009083; P:branched-chain amino acid catabolic process; IEA:EnsemblPlants.
DR   GO; GO:0043617; P:cellular response to sucrose starvation; IEA:EnsemblPlants.
DR   GO; GO:0009646; P:response to absence of light; IEA:EnsemblPlants.
DR   GO; GO:0009744; P:response to sucrose; IEA:EnsemblPlants.
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:UP000029120}.
FT   DOMAIN          37..212
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   357 AA;  39300 MW;  34D9218502E1AFD5 CRC64;
     MAGLLGRLSR RSSFPVSGHG IRMFSTVEHV SENGKSMNLY SAINQALHIA LETDPRSYVF
     GEDVGFGGVF RCTTGLAERF GKSRVFNTPL CEQGIVGFGI GLAAMGNRVI AEIQFADYIF
     PAFDQIVNEA AKFRYRSGNQ FNCGGLTIRA PYGAVGHGGH YHSQSPEAFF CHVPGIKVVI
     PRSPREAKGL LLSSIRDPNP VVFFEPKWLY RQAVEDVPED DYMIPLSEAE VIREGSDITL
     VGWGAQLTIM EQACLDAEKE GISCELIDLK TLIPWDKEIV ETSVRKTGRL LISHEAPVTG
     GFGAEIAATI VERCFLRLEA PVSRVCGLDT PFPLVFEPFY MPTKNKILDA IKSTVNY
//
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