ID U6KR05_EIMTE Unreviewed; 403 AA.
AC U6KR05;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ETH_00025495 {ECO:0000313|EMBL:CDJ37838.1};
OS Eimeria tenella (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5802 {ECO:0000313|EMBL:CDJ37838.1};
RN [1] {ECO:0000313|EMBL:CDJ37838.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ37838.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ37838.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ37838.1};
RA Aslett M.;
RL Submitted (OCT-2013) 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; HG673782; CDJ37838.1; -; Genomic_DNA.
DR RefSeq; XP_013228676.1; XM_013373222.1.
DR AlphaFoldDB; U6KR05; -.
DR EnsemblProtists; CDJ37838; CDJ37838; ETH_00025495.
DR GeneID; 25254209; -.
DR VEuPathDB; ToxoDB:ETH2_0522700; -.
DR VEuPathDB; ToxoDB:ETH_00025495; -.
DR OMA; SEAYYMA; -.
DR OrthoDB; 364at2759; -.
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;
FT DOMAIN 83..258
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 403 AA; 43681 MW; 57801FE74D41BFEF CRC64;
MAPHAASRFL SLLTPAPLSR VCLNRGPLAS FRAPSLASVP LHATWGPNSS QKRGFAHGPG
TDLTVACRTS TSPRPDHGPT TSMNLFTAIN SAMHIALETD PTACVFGEDV AFGGVFRCSV
DLRDKFGHHR VFNTPLSEQG IAGMAVGMAA VGYTAIAEIQ FGDYIFPAFD QIVNEAAKFR
YRSGNNWNCG KVTFRSSWGA VGHGGLYHSQ SPEAFFAHAA GLKIVIPRGP YQAKGLLLSC
IRDENPCLFF EPKALYRVAT DEVPTGDYML DLSKADVLKE GEHVTAVAWG TQVHRVLRAA
ELVAAEGVSV EVIDLQTIAP WDVDTVAASV RKTGRLLVSH EAQQTMGFAA EVAAAIQEKC
FFSLEAPIKR VTGYDTPFPL AYEPFYLPNE WKLADAMREL KAH
//
