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Database: UniProt
Entry: W5LBV9_ASTMX
LinkDB: W5LBV9_ASTMX
Original site: W5LBV9_ASTMX 
ID   W5LBV9_ASTMX            Unreviewed;       397 AA.
AC   W5LBV9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 53.
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};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000017321.2, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000017321.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   AlphaFoldDB; W5LBV9; -.
DR   STRING; 7994.ENSAMXP00000017321; -.
DR   Ensembl; ENSAMXT00000017321.2; ENSAMXP00000017321.2; ENSAMXG00000016827.2.
DR   eggNOG; KOG0525; Eukaryota.
DR   GeneTree; ENSGT00940000156533; -.
DR   HOGENOM; CLU_012907_1_0_1; -.
DR   InParanoid; W5LBV9; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000016827; Expressed in head kidney and 14 other cell types or tissues.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..397
FT                   /note="3-methyl-2-oxobutanoate dehydrogenase (2-
FT                   methylpropanoyl-transferring)"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017182420"
FT   DOMAIN          76..251
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   397 AA;  43279 MW;  4C50362CF91F223A CRC64;
     MARSSGVVCV CMMAAVRLLL RTVSSASSCA HSGSGTALLR FSPTCSSRPR AQRRHAAHFA
     FHPDPVPTKY GPTVKMNLFQ SITSALDNTL ASDPTAVIFG EDVAFGGVFR CTVGLRDKYG
     KDRVFNTPLC EQGIVGFGIG VAVAGATAIA EIQFADYIFP AFDQIVNEAA KYRYRSGNLY
     DCGNLTIRAP WGCVGHGSLY HSQSPEAYFA HCPGLKVVVP RGPVQAKGLL LSCIADENPC
     IFFEPKILYR AAVEQVPTEP YHLPLSQAEV VQEGSDVTLV AWGTQVHVMR EVATMAQEKL
     GVSCEVIDLQ TILPWDIETV CKSVVKTGRL LISHEAPVTG GFAAEISSSI QEQCFLNLEA
     PIARVCGYDT PFPHIFEPFY IPDKWKCFEA VKRMINY
//
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