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Database: UniProt
Entry: N6VVQ5_9GAMM
LinkDB: N6VVQ5_9GAMM
Original site: N6VVQ5_9GAMM 
ID   N6VVQ5_9GAMM            Unreviewed;       221 AA.
AC   N6VVQ5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=phosphoglycolate phosphatase {ECO:0000256|ARBA:ARBA00013078};
DE            EC=3.1.3.18 {ECO:0000256|ARBA:ARBA00013078};
GN   ORFNames=J139_18716 {ECO:0000313|EMBL:ENN97251.1};
OS   Pseudoalteromonas agarivorans S816.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1307437 {ECO:0000313|EMBL:ENN97251.1, ECO:0000313|Proteomes:UP000012320};
RN   [1] {ECO:0000313|EMBL:ENN97251.1, ECO:0000313|Proteomes:UP000012320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S816 {ECO:0000313|EMBL:ENN97251.1,
RC   ECO:0000313|Proteomes:UP000012320};
RA   Vynne N.G., Gram L.;
RT   "Comparative genomics of marine Pseudoalteromonads.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Organic acid metabolism; glycolate biosynthesis; glycolate
CC       from 2-phosphoglycolate: step 1/1. {ECO:0000256|ARBA:ARBA00004818}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       CbbY/CbbZ/Gph/YieH family. {ECO:0000256|ARBA:ARBA00006171}.
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:ENN97251.1}.
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DR   EMBL; APME01000074; ENN97251.1; -; Genomic_DNA.
DR   RefSeq; WP_004589357.1; NZ_APME01000074.1.
DR   AlphaFoldDB; N6VVQ5; -.
DR   PATRIC; fig|1307437.4.peg.3803; -.
DR   eggNOG; COG0546; Bacteria.
DR   Proteomes; UP000012320; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ   SEQUENCE   221 AA;  24466 MW;  18D43902E7991B91 CRC64;
     MKYDVALFDL DGTLVDSVYD LYLAVNLTLS DLAFPIVSQS LVESWIGNGI ETLVKRALSG
     DMQISEHLDE ALSAKAIALF YQHYEQLVGK YSVLYQHVET GLSALRGMPK ALVTNKARLF
     TELLLDKLSL TSHFEVIVCG DDMAKKPSPA PLLYACKKLN VEPSKAIMIG DSKSDILAAH
     AAKIDVIAVD YGYNQGENLE DYNPQYLCDN FLDIIPTLTQ R
//
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