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
//