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Database: UniProt
Entry: A0A120CUW5_HYPSL
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ID   A0A120CUW5_HYPSL        Unreviewed;       245 AA.
AC   A0A120CUW5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Phosphoglycolate phosphatase {ECO:0000256|ARBA:ARBA00013078, ECO:0000256|HAMAP-Rule:MF_00495};
DE            Short=PGP {ECO:0000256|HAMAP-Rule:MF_00495};
DE            Short=PGPase {ECO:0000256|HAMAP-Rule:MF_00495};
DE            EC=3.1.3.18 {ECO:0000256|ARBA:ARBA00013078, ECO:0000256|HAMAP-Rule:MF_00495};
GN   ORFNames=APY04_2289 {ECO:0000313|EMBL:KWT66882.1};
OS   Hyphomicrobium sulfonivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=121290 {ECO:0000313|EMBL:KWT66882.1, ECO:0000313|Proteomes:UP000059074};
RN   [1] {ECO:0000313|EMBL:KWT66882.1, ECO:0000313|Proteomes:UP000059074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WDL6 {ECO:0000313|EMBL:KWT66882.1,
RC   ECO:0000313|Proteomes:UP000059074};
RA   Albers P.;
RT   "Transcriptomic analysis of a linuron degrading triple-species bacterial
RT   consortium.";
RL   Submitted (OCT-2015) 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:0000256|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:0000256|ARBA:ARBA00000830, ECO:0000256|HAMAP-
CC         Rule:MF_00495};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_00495};
CC   -!- PATHWAY: Organic acid metabolism; glycolate biosynthesis; glycolate
CC       from 2-phosphoglycolate: step 1/1. {ECO:0000256|ARBA:ARBA00004818,
CC       ECO:0000256|HAMAP-Rule:MF_00495}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       CbbY/CbbZ/Gph/YieH family. {ECO:0000256|ARBA:ARBA00006171,
CC       ECO:0000256|HAMAP-Rule:MF_00495}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KWT66882.1}.
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DR   EMBL; LMTR01000071; KWT66882.1; -; Genomic_DNA.
DR   RefSeq; WP_068462541.1; NZ_LMTR01000071.1.
DR   AlphaFoldDB; A0A120CUW5; -.
DR   STRING; 121290.APY04_2289; -.
DR   PATRIC; fig|121290.4.peg.2487; -.
DR   OMA; YLCGKFG; -.
DR   OrthoDB; 9793014at2; -.
DR   UniPathway; UPA00865; UER00834.
DR   Proteomes; UP000059074; Unassembled WGS sequence.
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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   HAMAP; MF_00495; GPH_hydrolase_bact; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   InterPro; IPR037512; PGPase_prok.
DR   NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR   NCBIfam; TIGR01449; PGP_bact; 1.
DR   PANTHER; PTHR43434; PHOSPHOGLYCOLATE PHOSPHATASE; 1.
DR   PANTHER; PTHR43434:SF15; PHOSPHOGLYCOLATE PHOSPHATASE; 1.
DR   Pfam; PF13419; HAD_2; 1.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SFLD; SFLDG01135; C1.5.6:_HAD__Beta-PGM__Phospha; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_00495};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00495};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00495};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00495}; Reference proteome {ECO:0000313|Proteomes:UP000059074}.
FT   ACT_SITE        9
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00495"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00495"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00495"
FT   BINDING         171
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00495"
SQ   SEQUENCE   245 AA;  25847 MW;  3B77875F29D5F12D CRC64;
     MTDLTLVFDL DGTLVDSAPD LIASTNHVLD HLGLARVDAA TLRPFVGHGA KHMIEKAIGP
     ACEKLSEAER AALLKRYLDF YSANIATGSR PFAGVVPALQ NLRAEGVRLA VCTNKMEGMA
     QRLLDALDMT HYFTAIAGRD TFPVSKPDPG ALLGTIALAG GDRSHAIMVG DTNVDIAAAK
     AASVPVIGVT FGYTETPVQA FGPDAVIEHF AELEQAIGML VSRRQQASVT ADADESSRLA
     RAVAH
//
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