ID U6MTF9_9EIME Unreviewed; 326 AA.
AC U6MTF9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Pyruvate dehydrogenase E1 beta subunit, putative {ECO:0000313|EMBL:CDJ66373.1};
DE Flags: Fragment;
GN ORFNames=ENH_00019400 {ECO:0000313|EMBL:CDJ66373.1};
OS Eimeria necatrix.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51315 {ECO:0000313|EMBL:CDJ66373.1};
RN [1] {ECO:0000313|EMBL:CDJ66373.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ66373.1};
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:CDJ66373.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ66373.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|ARBA:ARBA00025211}.
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DR EMBL; HG723571; CDJ66373.1; -; Genomic_DNA.
DR RefSeq; XP_013434841.1; XM_013579387.1.
DR AlphaFoldDB; U6MTF9; -.
DR GeneID; 25472113; -.
DR VEuPathDB; ToxoDB:ENH_00019400; -.
DR OrthoDB; 5473567at2759; -.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
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; IPR033248; Transketolase_C.
DR PANTHER; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1.
DR PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Pyruvate {ECO:0000313|EMBL:CDJ66373.1}.
FT DOMAIN 56..117
FT /note="Transketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02780"
FT REGION 134..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CDJ66373.1"
SQ SEQUENCE 326 AA; 34765 MW; 024FBE10D4DE0ACD CRC64;
AVPGLKLVAC STPFNARGLL KSAIREDNPV VFFEHVLNYS NSDLIPLNPY TLSLEKAEKV
AAGEDLTVLC YGRLRQVAAA ALQQLQQLGV NPDLVDLISL KPLDLQTIRA SLKTTKRKSN
SSSRDSFAAA VEAATATAAA APNGRKQQQP QQQQQQQQQQ QQWKLVELRA IFVEFAEVPG
QPQQQQQLQQ QQQLQKHQQQ PQQQLQRPQQ QQLKEPQQQQ QRQQQQQQQQ QHRQGRVVSC
GELCGLGSAD SLTQTYLNPT AWPPAAAAAA AAAAEAAAAA AAAAAAEAAA AAAAAAPAPA
AAAAAARASN SCFLFVCTLS LGSSAS
//
