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Database: UniProt
Entry: U6M150_EIMMA
LinkDB: U6M150_EIMMA
Original site: U6M150_EIMMA 
ID   U6M150_EIMMA            Unreviewed;       615 AA.
AC   U6M150;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE            EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN   ORFNames=EMWEY_00024400 {ECO:0000313|EMBL:CDJ56818.1};
OS   Eimeria maxima (Coccidian parasite).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5804 {ECO:0000313|EMBL:CDJ56818.1};
RN   [1] {ECO:0000313|EMBL:CDJ56818.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Weybridge {ECO:0000313|EMBL:CDJ56818.1};
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:CDJ56818.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Weybridge {ECO:0000313|EMBL:CDJ56818.1};
RA   Aslett M.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC         EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231}.
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DR   EMBL; HG719125; CDJ56818.1; -; Genomic_DNA.
DR   RefSeq; XP_013333468.1; XM_013478014.1.
DR   AlphaFoldDB; U6M150; -.
DR   EnsemblProtists; CDJ56818; CDJ56818; EMWEY_00024400.
DR   GeneID; 25336426; -.
DR   VEuPathDB; ToxoDB:EMWEY_00024400; -.
DR   OMA; WIQDRAN; -.
DR   OrthoDB; 5476118at2759; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR   Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR   InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR   InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR   InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR   InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   InterPro; IPR045244; PGM.
DR   PANTHER; PTHR22573:SF2; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
FT   DOMAIN          24..167
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          206..310
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          342..429
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   615 AA;  67612 MW;  3E87FADF3EFEEE31 CRC64;
     MTVKYSGVPA ESASVRATTP FEGQKPGTSG LRKKTREFMQ PGYLSNYVQA VFDCLPQSEV
     RGGTMLVAGD GRYFCDEAIK KIVAIAAGNG VGRVWIAKDG LASTPACSAI LRLREEGVAF
     GGFILTASHN PGGIDADFGV KYNTANGAPA LEGLTNQVYE RTKVIKEIKH VKLLDFDLDS
     YGVKVLIKEQ FMAEVIDGTE DWLRLMKAVF HFPALKRLLQ SPFSFVFDGM NGVAGPAAER
     LFVQELGAKP SCLRCCKPLP DFGGHHPDPN LEYAKELVEI MKIFSPEKVD SSTPLFGAAG
     DGDCDRNMIL GPGFFVTPSD SVAIIAMYAE KVIPFFMKNK DGSGGLKGVA RSMPTSMALD
     SVAKKLGKEL YETPTGWKYF TNLMDAGKLS ICGEESFGTG SVHVREKDGL WAVLCWLSIL
     AYRNGLMDNM QEELEMQKEG KLIPQTPPAT LENFVGVQQI VEEFWKEFGR NYYMRYDFEN
     KSSTAANEMM AALKLLTAGG KEALESHIKA TVPAELQSKL KAERIDVFKY TDPIDHSVAD
     NQGIRLFFPK GRAIWRLSGT GSSGATIRMY FELVEDKEDC LMKKPQEVLK DLIAYAIAFC
     KIKEYVGTDV PTVIT
//
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