GPH_SYNE7
ID GPH_SYNE7 Reviewed; 212 AA.
AC Q55039; Q31JX6;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Phosphoglycolate phosphatase;
DE Short=PGP;
DE Short=PGPase;
DE EC=3.1.3.18;
GN Name=cbbZ; OrderedLocusNames=Synpcc7942_2613;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8654968; DOI=10.1016/0378-1119(96)00160-6;
RA Liu Y., Tsinoremas N.F.;
RT "An unusual gene arrangement for the putative chromosome replication origin
RT and circadian expression of dnaN in Synechococcus sp. strain PCC 7942.";
RL Gene 172:105-109(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically catalyzes the dephosphorylation of 2-
CC phosphoglycolate. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Organic acid metabolism; glycolate biosynthesis; glycolate
CC from 2-phosphoglycolate: step 1/1.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB58643.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; U33322; AAA75108.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB58643.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q55039; -.
DR SMR; Q55039; -.
DR STRING; 1140.Synpcc7942_2613; -.
DR PRIDE; Q55039; -.
DR EnsemblBacteria; ABB58643; ABB58643; Synpcc7942_2613.
DR KEGG; syf:Synpcc7942_2613; -.
DR eggNOG; COG0546; Bacteria.
DR HOGENOM; CLU_045011_19_3_3; -.
DR BioCyc; SYNEL:SYNPCC7942_2613-MON; -.
DR UniPathway; UPA00865; UER00834.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046295; P:glycolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
PE 3: Inferred from homology;
KW Calvin cycle; Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW Photosynthesis.
FT CHAIN 1..212
FT /note="Phosphoglycolate phosphatase"
FT /id="PRO_0000108042"
FT ACT_SITE 7
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 157
FT /note="V -> D (in Ref. 1; AAA75108)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 212 AA; 23556 MW; 0254E18365DECED0 CRC64;
MQAIIFDFDG TLVDSLPTVV AIANAHAPDF GYDPIDERDY AQLRQWSSRT IVRRAGLSPW
QQARLLQRVQ RQLGDCLPAL QLFPGVADLL AQLRSRSLCL GILSSNSRQN IEAFLQRQGL
RSLFSVVQAG TPILSKRRAL SQLVAREGWQ PAAVMYVGDE TRDVEAARQV GLIAVAVTWG
FNDRQSLVAA CPDWLLETPS DLLQAVTQLM RQ