ID A0A1S3VFC4_VIGRR Unreviewed; 333 AA.
AC A0A1S3VFC4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Phosphoglycolate phosphatase 2 isoform X2 {ECO:0000313|RefSeq:XP_014516912.1};
GN Name=LOC106774434 {ECO:0000313|RefSeq:XP_014516912.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014516912.1};
RN [1] {ECO:0000313|RefSeq:XP_014516912.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014516912.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000915-3};
CC Note=Divalent metal ions. Mg(2+) is the most effective.
CC {ECO:0000256|PIRSR:PIRSR000915-3};
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DR RefSeq; XP_014516912.1; XM_014661426.2.
DR AlphaFoldDB; A0A1S3VFC4; -.
DR GeneID; 106774434; -.
DR KEGG; vra:106774434; -.
DR OrthoDB; 217676at2759; -.
DR Proteomes; UP000087766; Chromosome 10.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR CDD; cd07510; HAD_Pase_UmpH-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006349; PGP_euk.
DR NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR NCBIfam; TIGR01452; PGP_euk; 1.
DR PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR19288:SF75; PHOSPHOGLYCOLATE PHOSPHATASE 2; 1.
DR Pfam; PF13344; Hydrolase_6; 1.
DR Pfam; PF13242; Hydrolase_like; 1.
DR PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00039; phosphoglycolate_phosphatase_2; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000915-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000915-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766}.
FT ACT_SITE 24
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT ACT_SITE 26
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT BINDING 24
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 26
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ SEQUENCE 333 AA; 36640 MW; 7601ABD9B3EEAC4D CRC64;
MSSQPLSPSN FKDLFDSVEA FLFDCDGVIW KGDELIQGVP KTLQMLRSKG KKLVFVTNNS
WKSRSQYAQK FQSLGISVSQ DEIFSSSFAA AMYLKAKDFP SQNKVYVIGG EGILEELQLA
GITAFGGPED ANKTIDLKQN CFVEHDKSVG AVVVGIDPNI NYYKLQYGTL CIRENPGCLF
IATNRDAVGH MTALQEWPGA GCMVAAICGS TQKEPVVVGK PSTFMMEFLL KKFNVSCSKM
CMVGDRLDTD ILFGQNAGCK TLLVLSGVTT QSALQDPSNN IQPDYYTNTI SDMVDLSKLI
SGSLLHHFVV RWFAPSIKLK RYGCSPLRSR TIL
//