ID A0A0J7NTE5_LASNI Unreviewed; 120 AA.
AC A0A0J7NTE5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=RF55_4074 {ECO:0000313|EMBL:KMQ95695.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ95695.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMQ95695.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMQ95695.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-2015) 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};
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:KMQ95695.1}.
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DR EMBL; LBMM01001817; KMQ95695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7NTE5; -.
DR STRING; 67767.A0A0J7NTE5; -.
DR PaxDb; 67767-A0A0J7NTE5; -.
DR OrthoDB; 5473567at2759; -.
DR Proteomes; UP000036403; Unassembled WGS sequence.
DR Gene3D; 3.40.50.970; -; 1.
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; PF02779; Transket_pyr; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Pyruvate {ECO:0000313|EMBL:KMQ95695.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036403}.
FT DOMAIN 3..120
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 120 AA; 13185 MW; 5B6BAB9CADC3FEA6 CRC64;
MKRNNVQAIS LALELAMKKH NNVLVYGEDV GNVGGVFRAT RGLQKKFGVE RCFDAPIAEA
LIAGTAVGAS INGMRPVIEM QFSGFAYPAF QQLLAHAARM RNRSRGRYTC PLVVRLPSYD
//
