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Database: UniProt
Entry: B8BUT0_THAPS
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Original site: B8BUT0_THAPS 
ID   B8BUT0_THAPS            Unreviewed;       814 AA.
AC   B8BUT0;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=THAPSDRAFT_21344 {ECO:0000313|EMBL:EED95340.1};
OS   Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=35128 {ECO:0000313|EMBL:EED95340.1, ECO:0000313|Proteomes:UP000001449};
RN   [1] {ECO:0000313|EMBL:EED95340.1, ECO:0000313|Proteomes:UP000001449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 {ECO:0000313|EMBL:EED95340.1};
RX   PubMed=15459382; DOI=10.1126/science.1101156;
RA   Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA   Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA   Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA   Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA   Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA   Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA   Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA   Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA   Wilkerson F.P., Rokhsar D.S.;
RT   "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT   metabolism.";
RL   Science 306:79-86(2004).
RN   [2] {ECO:0000313|EMBL:EED95340.1, ECO:0000313|Proteomes:UP000001449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 {ECO:0000313|EMBL:EED95340.1};
RX   PubMed=18923393; DOI=10.1038/nature07410;
RA   Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA   Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA   Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA   Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA   Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA   Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA   Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA   La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA   Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA   Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA   Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA   Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA   Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA   Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "The Phaeodactylum genome reveals the evolutionary history of diatom
RT   genomes.";
RL   Nature 456:239-244(2008).
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; CM000639; EED95340.1; -; Genomic_DNA.
DR   RefSeq; XP_002287897.1; XM_002287861.1.
DR   AlphaFoldDB; B8BUT0; -.
DR   STRING; 35128.B8BUT0; -.
DR   PaxDb; 35128-Thaps21344; -.
DR   EnsemblProtists; EED95340; EED95340; THAPSDRAFT_21344.
DR   GeneID; 7446632; -.
DR   KEGG; tps:THAPSDRAFT_21344; -.
DR   eggNOG; KOG1182; Eukaryota.
DR   HOGENOM; CLU_347015_0_0_1; -.
DR   InParanoid; B8BUT0; -.
DR   OMA; QCPPAVG; -.
DR   Proteomes; UP000001449; Chromosome 2.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR   GO; GO:0009083; P:branched-chain amino acid catabolic process; IBA:GO_Central.
DR   GO; GO:0007584; P:response to nutrient; IBA:GO_Central.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001449}.
FT   DOMAIN          488..662
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   814 AA;  89458 MW;  CC8D8BC7D9DA1187 CRC64;
     MVMIHLYHTH RAATLQTALR ASFSSTSSDI NPTTGILERL QKQAQSDILA LPECKARSDL
     YNFLSSKAGI PPQHPHTILD ITPPKLPSSG YKHVLTQPQI LMSLDAAMAT FHLHVESRIA
     ALCAQGFYTI GPCGEEMLAS IGFALDPHVD AMALHYRHLS VSVVRQLRLG KKSLEDIILD
     RARGYVVSKL DPVTGGVHCA IGSAIDPSID DNGGGDYVVT STLASQCPPA VGRALGFSVA
     DTIFQRNNPP SKKQVSFVTV GDGSIHNAHF LSAFNLARHA RYRRTKCPVV FGVSDNGLSI
     SYSTDGYADF LFTKSQSNPQ ATKQRDGIPL FKANGSDMFD VYDKTMQATA YSRKNSAPAL
     VLYQALIRRF GHAATDRQHA YLDASVVDRM AESDVVASGI VQAVEQWSAL TYSEALDRFH
     EIGQVVKRSF ISAAEEPKIT KRDDMIDRVS QLMMSVPRLP SDILVSSASD MFHSIQSDVK
     PTEREKRDVM RKQMTRCIGE AMESNVNVVY IGEDVKHGGY YLVTDGLASR FPGRVIDFPP
     DETTLLGAAM GFSHVGLVPI VEIPYAKYLD CGADMFYELA ISNWLTNKQR PNGMIVRVQG
     FDKGVFGGNF HTHNMLSHIP PGVDVVCYSN GEDYVRGMRN AIVQAQSGRV VVVVDCTNLL
     NLRHLHSKDR GWETAYPTSK GNGMMSFHDV RQFGSTGKHL IVTYGNGVVT ALRARRQLAE
     QQGISEDEID IIDCPYLSDV PDGLREILSR DQYSDGAILF ADICKEGPGS NPLSSMIMAL
     RKDNLLPAKW GFKCEQSQKK SFANSSANSD NDEF
//
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