GPH_AQUAE
ID GPH_AQUAE Reviewed; 213 AA.
AC O67359;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Phosphoglycolate phosphatase;
DE Short=PGP;
DE Short=PGPase;
DE EC=3.1.3.18;
GN Name=gph; OrderedLocusNames=aq_1342;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-213 IN COMPLEX WITH SUBSTRATE
RP ANALOGS, AND SUBUNIT.
RG New York structural genomix research consortium (NYSGXRC);
RT "X-ray crystal structure of a phosphoglycolate phosphatase from Aquifex
RT aeolicus.";
RL Submitted (FEB-2009) to the PDB data bank.
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 -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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DR EMBL; AE000657; AAC07313.1; -; Genomic_DNA.
DR PIR; D70416; D70416.
DR RefSeq; NP_213923.1; NC_000918.1.
DR RefSeq; WP_010880861.1; NC_000918.1.
DR PDB; 2NYV; X-ray; 2.10 A; A=2-213.
DR PDB; 2YY6; X-ray; 2.30 A; A/B=1-213.
DR PDBsum; 2NYV; -.
DR PDBsum; 2YY6; -.
DR AlphaFoldDB; O67359; -.
DR SMR; O67359; -.
DR STRING; 224324.aq_1342; -.
DR PRIDE; O67359; -.
DR EnsemblBacteria; AAC07313; AAC07313; aq_1342.
DR KEGG; aae:aq_1342; -.
DR eggNOG; COG0546; Bacteria.
DR HOGENOM; CLU_045011_19_1_0; -.
DR InParanoid; O67359; -.
DR OMA; YLCGKFG; -.
DR OrthoDB; 1562270at2; -.
DR BRENDA; 3.1.3.18; 396.
DR UniPathway; UPA00865; UER00834.
DR EvolutionaryTrace; O67359; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
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; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR037512; PGPase_prok.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..213
FT /note="Phosphoglycolate phosphatase"
FT /id="PRO_0000108025"
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 38..39
FT /ligand="substrate"
FT BINDING 43
FT /ligand="substrate"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2NYV"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:2NYV"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:2NYV"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2NYV"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:2NYV"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:2NYV"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:2NYV"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:2NYV"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:2NYV"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:2NYV"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:2NYV"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2NYV"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:2NYV"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:2YY6"
FT HELIX 141..150
FT /evidence="ECO:0007829|PDB:2NYV"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2NYV"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:2NYV"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:2NYV"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:2NYV"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:2NYV"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:2NYV"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:2NYV"
SQ SEQUENCE 213 AA; 23896 MW; 0722EC7F6BE4B753 CRC64;
MRVILFDLDG TLIDSAKDIA LALEKTLKEL GLEEYYPDNV TKYIGGGVRA LLEKVLKDKF
REEYVEVFRK HYLENPVVYT KPYPEIPYTL EALKSKGFKL AVVSNKLEEL SKKILDILNL
SGYFDLIVGG DTFGEKKPSP TPVLKTLEIL GEEPEKALIV GDTDADIEAG KRAGTKTALA
LWGYVKLNSQ IPDFTLSRPS DLVKLMDNHI VEF
