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Database: UniProt
Entry: B9PVD0_TOXGV
LinkDB: B9PVD0_TOXGV
Original site: B9PVD0_TOXGV 
ID   B9PVD0_TOXGV            Unreviewed;       597 AA.
AC   B9PVD0; A0A0F7UQN9; B9QI47; S7UKB6;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   SubName: Full=Glucosephosphate-mutase GPM2 {ECO:0000313|EMBL:ESS29726.1};
DE            EC=2.7.1.106 {ECO:0000313|EMBL:ESS29726.1};
DE   SubName: Full=Phosphoglucomutase, putative {ECO:0000313|EMBL:CEL72535.1};
GN   ORFNames=BN1205_009980 {ECO:0000313|EMBL:CEL72535.1}, TGVEG_318580
GN   {ECO:0000313|EMBL:ESS29726.1};
OS   Toxoplasma gondii (strain ATCC 50861 / VEG).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX   NCBI_TaxID=432359 {ECO:0000313|EMBL:ESS29726.1, ECO:0000313|Proteomes:UP000002226};
RN   [1] {ECO:0000313|EMBL:ESS29726.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VEG {ECO:0000313|EMBL:ESS29726.1};
RA   Paulsen I.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50861 / VEG {ECO:0000313|Proteomes:UP000002226};
RA   Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT   "Annotation of Toxoplasma gondii VEG.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ESS29726.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VEG {ECO:0000313|EMBL:ESS29726.1};
RA   Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B.,
RA   Roos D., Caler E., Lorenzi H.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:CEL72535.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VEG {ECO:0000313|EMBL:CEL72535.1};
RX   PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA   Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA   Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT   "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT   Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT   Transcript Features.";
RL   PLoS ONE 10:e0124473-e0124473(2015).
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, ECO:0000256|RuleBase:RU004326}.
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DR   EMBL; LN714493; CEL72535.1; -; Genomic_DNA.
DR   EMBL; AAYL02000285; ESS29726.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9PVD0; -.
DR   STRING; 432359.B9PVD0; -.
DR   PaxDb; 5811-TGME49_118580; -.
DR   EnsemblProtists; ESS29726; ESS29726; TGVEG_318580.
DR   VEuPathDB; ToxoDB:TGVEG_318580; -.
DR   eggNOG; KOG1220; Eukaryota.
DR   OMA; PQDNGYK; -.
DR   Proteomes; UP000002226; Partially assembled WGS sequence.
DR   GO; GO:0047933; F:glucose-1,6-bisphosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05799; PGM2; 1.
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; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR   PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 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;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004326};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002226};
KW   Transferase {ECO:0000313|EMBL:ESS29726.1}.
FT   DOMAIN          53..191
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          229..334
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          344..464
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          532..569
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   597 AA;  65896 MW;  E9CBAFB6D0956686 CRC64;
     MSVANRKFVN GALEAAVNFW RSVDRREETQ KETLELLKNL TEDELAKLFL ARLEFGTAGL
     RGRMGAGFSR MNDVTIQQTT QGYCAFLVDV FGEDGKDRGV VIGFDARHNS RRFAQLTAAV
     FLSKGFRVQL FSDIVHTPMV PYTVVAANCI AGIMITASHN PKADNGYKVY AANGAQIIPP
     MDSEISAFIN SNLDFWSDVD EYFDSKTGML TEKAANSSLL EDPLNTYVDA YIKDIAADLC
     VAEQQGSDLK FMYTAMHGVG TPMVKKMLAA FGFNDNLLTV DAQCTPDPEF PTVAFPNPEE
     KGALDLAFQE ADSHGLTLVI ANDPDADRFA AAEKCDGRWY QFTGDELGAI LGAYAIKLRE
     GQGISKSKMA LICSAVSSRM LQKIAKENGC TFAETMTGFK WMENKAIEME AEGLIPVFVY
     EEALGYALSQ RVRDKDGVSA AAVWMQMAID LYSRGQTVMD FLMSLRKRYG YFVTRNSYFI
     CPDPRLIQGL FKDFANGGNY PKQLGPFTIR RIRDVGRGYD SEEQCSFPSN CEMLTVYLDN
     GAVVTLRGSG TEPKLKYYAE TSSTDPEQGL AELAKVIAAV ISDFVKPEIH PAIQVTL
//
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