ID A0A384BKE7_URSMA Unreviewed; 438 AA.
AC A0A384BKE7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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 Name=BCKDHB {ECO:0000313|RefSeq:XP_008683082.1,
GN ECO:0000313|RefSeq:XP_008683083.1, ECO:0000313|RefSeq:XP_008683084.1};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008683083.1};
RN [1] {ECO:0000313|RefSeq:XP_008683082.1, ECO:0000313|RefSeq:XP_008683083.1}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008683082.1,
RC ECO:0000313|RefSeq:XP_008683083.1};
RG RefSeq;
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 RefSeq; XP_008683082.1; XM_008684860.2.
DR RefSeq; XP_008683083.1; XM_008684861.2.
DR RefSeq; XP_008683084.1; XM_008684862.2.
DR GeneID; 103657422; -.
DR CTD; 594; -.
DR OrthoDB; 364at2759; -.
DR Proteomes; UP000261680; Unplaced.
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; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000261680}.
FT DOMAIN 71..246
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 438 AA; 48104 MW; 424967EF131179F4 CRC64;
MAAFAATAGG LLRLRAAGSE GQWRRLRGAG LLRGLLQPES ATGVAAQRRR VAHFTFQPDP
EPREYGQTQK MNLFQAITSA LDNSLAKDPT AVIFGEDVAF GGVFRCTVGL RDKYGKDRVF
NTPLCEQGIV GFGIGIAVTG ATAIAEIQFA DYIFPAFDQI VNEAAKYRYR SGDLFNCGSL
TIRAPWGCVG HGALYHSQSP EAFFAHCPGI KVVVPRSPFQ AKGLLLSCIE DKNPCIFFEP
KILYRAAVEQ VPVEPYNVPL SQAEVIQEGS DVTLVAWGTQ VHVIREVAAM AQEKLGVSCE
VIDLRTILPW DVDTVCKSVI KTGRLLISHE APLTGGFASE ISSTVQDRDR TFALQLCFTV
ISLAHSVIVL EGEETLQIPF GNSEVTEIPT AEEECFLNLE APISRVCGYD TPFPHIFEPF
YIPDKWKCYD ALRKMINY
//
