ID A0A2A5CW73_9GAMM Unreviewed; 217 AA.
AC A0A2A5CW73;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=COA99_00200 {ECO:0000313|EMBL:PCJ47795.1};
OS Moraxellaceae bacterium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae.
OX NCBI_TaxID=1889775 {ECO:0000313|EMBL:PCJ47795.1, ECO:0000313|Proteomes:UP000218379};
RN [1] {ECO:0000313|Proteomes:UP000218379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-2017) 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:PCJ47795.1}.
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; NVVG01000002; PCJ47795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5CW73; -.
DR UniPathway; UPA00865; UER00834.
DR Proteomes; UP000218379; 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 CDD; cd16417; HAD_PGPase; 1.
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; TIGR01509; HAD-SF-IA-v3; 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 SFLD; SFLDG01135; C1.5.6:_HAD__Beta-PGM__Phospha; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 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}.
FT ACT_SITE 2
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00495"
FT BINDING 2
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00495"
FT BINDING 4
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00495"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00495"
SQ SEQUENCE 217 AA; 23636 MW; 1A571AE0ED7352AF CRC64;
MDLDGTLVDS VPDLAKAIDQ MLSQLGRQPA GEQNIRRWVG EGAEQLVRRA LAKDGSDAQA
AKVSETLLAN AMSCFFQNYT LCNGSHSLLY PAVIDTLKAL KNKAIPMALV TNKPAQFTAP
LLAQFGLDPY FDVVVSGDSL EHKKPHPEPL LYAAMRLQAN PINCVMVGDS RSDVEAARAA
FFKVVCVDYG YNHGEPISQC NPDCLIESLD ELVQGWL
//