ID A0A0P5SYC6_9CRUS Unreviewed; 317 AA.
AC A0A0P5SYC6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=APZ42_034440 {ECO:0000313|EMBL:KZS02999.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:JAL65413.1};
RN [1] {ECO:0000313|EMBL:JAL65413.1}
RP NUCLEOTIDE SEQUENCE.
RA Gilbert D., Podicheti R., Orsini L., Colbourne J., Pfrender M.;
RT "Daphnia magna gene sets from two clonal populations assembled and
RT annotated with EvidentialGene.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAL65413.1}
RP NUCLEOTIDE SEQUENCE.
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KZS02999.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS02999.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS02999.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; GDIP01138301; JAL65413.1; -; Transcribed_RNA.
DR EMBL; LRGB01003375; KZS02999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P5SYC6; -.
DR STRING; 35525.A0A0P5SYC6; -.
DR EnsemblMetazoa; XM_032931445.2; XP_032787336.2; LOC116924860.
DR Proteomes; UP000076858; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000076858}.
FT DOMAIN 44..219
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 317 AA; 34788 MW; 6F40D4FFD26EA932 CRC64;
MALRNFLTRN LLLNKCPLRI SQRLSHFTFV PDTVSASEGE TQRMNLFQAI NNSLDLALSS
DPTAIIFGED VAFGGVFRCT VGLQEKHGKS RVFNTPLCEQ GIAGFGIGAA TAGATAIAEI
QFADYILPAF DQICNEAAKY RYRSGGLYDC GSLTIRAPCS AVGHGALYHS QSPEAFFAHC
PGLKVVVPRG PIKAKGLLLS CIRDKNPCLF FEPKILYRSA VEQVPVKEYT MPLSKADILV
EGDDITLVGW GTQVHVLREV CQLAKDQLNV SCELIDLVTI LPWDKETIAQ VGNLNIMAFL
SFSLLQKKFL KWETLAI
//
