ID U6LUG8_9EIME Unreviewed; 231 AA.
AC U6LUG8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 28-JUN-2023, entry version 29.
DE RecName: Full=phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) {ECO:0000256|ARBA:ARBA00012028};
DE EC=5.4.2.11 {ECO:0000256|ARBA:ARBA00012028};
GN ORFNames=EBH_0060760 {ECO:0000313|EMBL:CDJ53967.1};
OS Eimeria brunetti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51314 {ECO:0000313|EMBL:CDJ53967.1};
RN [1] {ECO:0000313|EMBL:CDJ53967.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ53967.1};
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:CDJ53967.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ53967.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717}.
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DR EMBL; HG713456; CDJ53967.1; -; Genomic_DNA.
DR AlphaFoldDB; U6LUG8; -.
DR EnsemblProtists; CDJ53967; CDJ53967; EBH_0060760.
DR VEuPathDB; ToxoDB:EBH_0060760; -.
DR OrthoDB; 9826at2759; -.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 2.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR11931:SF24; PHOSPHOGLYCERATE MUTASE (2,3-DIPHOSPHOGLYCERATE-DEPENDENT); 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235}.
FT REGION 28..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 231 AA; 24138 MW; 96EB8E67BDBEC3C2 CRC64;
MHRNMPVDLV LVRHGQSEGN LAQRLCRQQQ QQQQQQLQQQ QQQQQQQLQQ HTEGAAPPPP
PASPTAAAAA PAPPLASAAA ASASAAAGAS AAAAAAAAAA AAAAAAAGGP LVWSTEFRSR
HNSLYRLTDR GRRQAAIAGC WIRAHAGPPF DKYFTSEYVR AMETAATLDL PRLGAMETAA
TLDLPSARWP SGGESIANLC LRVDRVMENL AETCAGLRVL IVCHGGVING N
//
