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Database: UniProt
Entry: U6G3K0_9EIME
LinkDB: U6G3K0_9EIME
Original site: U6G3K0_9EIME 
ID   U6G3K0_9EIME            Unreviewed;       617 AA.
AC   U6G3K0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=EPH_0036200 {ECO:0000313|EMBL:CDI74801.1};
OS   Eimeria praecox.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=51316 {ECO:0000313|EMBL:CDI74801.1};
RN   [1] {ECO:0000313|EMBL:CDI74801.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDI74801.1};
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:CDI74801.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDI74801.1};
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; HG690547; CDI74801.1; -; Genomic_DNA.
DR   AlphaFoldDB; U6G3K0; -.
DR   EnsemblProtists; CDI74801; CDI74801; EPH_0036200.
DR   VEuPathDB; ToxoDB:EPH_0036200; -.
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          25..168
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          220..312
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          342..432
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   617 AA;  68162 MW;  2CEE7CBAE3A4F95D CRC64;
     MFSVKYSGVP AESASVRATT PFEGQKPGTS GLRKKTREFM QPGYLSNYVQ AVFDCLPESE
     VRGGTMLVAG DGRYFCDEAI KKIVAIAAGN GVGRVWIAKD GLASTPACSA ILRLREEGVA
     FGGFILTASH NPGGIDADFG VKYNTANGAP ALESLTNQVY ERTKVIKEIK HVKLLDFDLD
     SYGTKVLIKE QFMAEVIDGT EDWLRLMKAV FHFPALRRLV QSPSFSFVFD GMNGVAGPAA
     ERLFVQELGA KPTCLRCCKS LPDFGGHHPD PNLEYAKELV EIMKIFHPDK VDSKTPLFGA
     AGDGDCDRNM ILGPGFFVTP SDSVAIIAQY AEKVIPFFMK SKDGKGGIKG LARSMPTSMA
     LDSVAKKLGK EIYETPTGWK YFTNLMDAGR LSICGEESFG TGSVHVREKD GLWAVLCWLS
     ILAYRNGLME NIEEEMEMQK QGKTVSPTQP QPIQNFVGVQ QIVEEFWKEF GRNYYMRYDF
     ENKSSAAANE MMAALKQLTT GGQDALEKHI QATVPAELRS KLQAQRIDVF KYTDPIDNSV
     ADNQGIRLFF QNGRAIWRLS GTGSSGATIR MYFELVEERE DCLMKKPQEV LKDLIAYAIA
     FCKIKEYVGT DIPTVIT
//
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