ID A0A0R3X599_HYDTA Unreviewed; 251 AA.
AC A0A0R3X599;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|WBParaSite:TTAC_0000862501-mRNA-1};
GN ORFNames=TTAC_LOCUS8610 {ECO:0000313|EMBL:VDM33217.1};
OS Hydatigena taeniaeformis (Feline tapeworm) (Taenia taeniaeformis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Hydatigera.
OX NCBI_TaxID=6205 {ECO:0000313|Proteomes:UP000046396, ECO:0000313|WBParaSite:TTAC_0000862501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TTAC_0000862501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM33217.1, ECO:0000313|Proteomes:UP000274429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; UYWX01020544; VDM33217.1; -; Genomic_DNA.
DR STRING; 6205.A0A0R3X599; -.
DR WBParaSite; TTAC_0000862501-mRNA-1; TTAC_0000862501-mRNA-1; TTAC_0000862501.
DR Proteomes; UP000046396; Unplaced.
DR Proteomes; UP000274429; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR005952; Phosphogly_mut1.
DR NCBIfam; TIGR01258; pgm_1; 1.
DR PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Reference proteome {ECO:0000313|Proteomes:UP000274429}.
FT ACT_SITE 12
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 90
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 11..18
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 90..93
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 117..118
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 186..187
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT SITE 185
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ SEQUENCE 251 AA; 28398 MW; 9A00FB2686770FCE CRC64;
MGSVYKVVFI RHGESVYNQE NRFCGWHDAD LSPKGEQEAQ CAGKMIKENG LTFDIAFTSV
LKRAIKTLNH VLEVNDLHWI PVHKSWRLNE RMYGGLQGLN KSETAAKHGE DQVKIWRRAY
DIPPPPLEVS DKRWPGLEEK YKLLDVECIP VTECLKDTVE RALPFWFDAV VPAIKQGKRV
LITAHGNSLR AIVKFLDKIP DKDIVELNIP TGIPLVYELD KDLRPVKHYY LADDATVAAA
ISSVANQGKA K
//
