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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//