GPH_VIBVU
ID GPH_VIBVU Reviewed; 228 AA.
AC Q8DCT7;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Phosphoglycolate phosphatase {ECO:0000255|HAMAP-Rule:MF_00495};
DE Short=PGP {ECO:0000255|HAMAP-Rule:MF_00495};
DE Short=PGPase {ECO:0000255|HAMAP-Rule:MF_00495};
DE EC=3.1.3.18 {ECO:0000255|HAMAP-Rule:MF_00495};
GN Name=gph {ECO:0000255|HAMAP-Rule:MF_00495}; OrderedLocusNames=VV1_1306;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically catalyzes the dephosphorylation of 2-
CC phosphoglycolate. Is involved in the dissimilation of the intracellular
CC 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate
CC ends, a major class of DNA lesions induced by oxidative stress.
CC {ECO:0000255|HAMAP-Rule:MF_00495}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phosphoglycolate + H2O = glycolate + phosphate;
CC Xref=Rhea:RHEA:14369, ChEBI:CHEBI:15377, ChEBI:CHEBI:29805,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58033; EC=3.1.3.18;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00495};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00495};
CC -!- PATHWAY: Organic acid metabolism; glycolate biosynthesis; glycolate
CC from 2-phosphoglycolate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00495}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000255|HAMAP-Rule:MF_00495}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO09761.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE016795; AAO09761.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_043920933.1; NC_004459.3.
DR AlphaFoldDB; Q8DCT7; -.
DR SMR; Q8DCT7; -.
DR EnsemblBacteria; AAO09761; AAO09761; VV1_1306.
DR KEGG; vvu:VV1_1306; -.
DR HOGENOM; CLU_045011_19_1_6; -.
DR OMA; YLCGKFG; -.
DR UniPathway; UPA00865; UER00834.
DR Proteomes; UP000002275; Chromosome 1.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046295; P:glycolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_00495; GPH_hydrolase_bact; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR006346; PGPase/MupP.
DR InterPro; IPR037512; PGPase_prok.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
DR TIGRFAMs; TIGR01449; PGP_bact; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding.
FT CHAIN 1..228
FT /note="Phosphoglycolate phosphatase"
FT /id="PRO_0000108045"
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00495"
SQ SEQUENCE 228 AA; 24809 MW; AEF5B290CD905042 CRC64;
MTQQEIKLIA FDLDGTLLDS VPDLAVAADQ ATRAVGFPGV TELQVRDYVG NGADILIGRA
LSQSLTINPE LSDELRAQAR ELFDDFYQQT GHKLSHLYPT VKETLKELHQ AGFTLALVTN
KPSKFVPDVL QQHGIADYFV DVLGGDSFPE KKPNPIALNW LMEKHQIQPT EMLMVGDSKN
DILAAKNAGC ASFGLTYGYN HGEPIAASEP DFVADSLAQL LDVVLVSA