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Q9HLQ2 (PGP_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoglycolate phosphatase
Short name=PGP
Short name=PGPase
EC=3.1.3.18
Gene names
Ordered Locus Names:Ta0175
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the dephosphorylation of 2-phosphoglycolate. Also has significant, but less efficient, pyrophosphatase activity, since it is able to catalyze the release of phosphate from inorganic pyrophosphate (PPi). Ref.2

Catalytic activity

2-phosphoglycolate + H2O = glycolate + phosphate. HAMAP MF_01419

Cofactor

Binds 5 magnesium ions per homodimer. Ref.2

Enzyme regulation

Inhibited by Ca2+ ions and by high chloride ion concentration. By contrast, low chloride concentration (up to 50 mM) slightly activate the enzyme. HAMAP MF_01419

Subunit structure

Homodimer. Ref.2

Sequence similarities

Belongs to the HAD-like hydrolase superfamily. Archaeal SPP-like hydrolase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.037 mM for 2-phosphoglycolate Ref.2

KM=3.1 mM for pNPP

KM=0.17 mM for pyrophosphate

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

phosphoglycolate phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 224224Phosphoglycolate phosphatase HAMAP MF_01419
PRO_0000146731

Sites

Active site81Nucleophile
Metal binding81Magnesium 1
Metal binding101Magnesium 3
Metal binding111Magnesium 2; via carbonyl oxygen
Metal binding431Magnesium 3; via amide nitrogen
Metal binding1741Magnesium 1
Metal binding1741Magnesium 2
Metal binding1751Magnesium 1
Metal binding1781Magnesium 1
Binding site1511Substrate By similarity

Secondary structure

1 ................................................ 224
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9HLQ2 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: E98BE17558DE72E9

FASTA22425,279
        10         20         30         40         50         60 
MIRLAAIDVD GTLTDRDRLI STKAIESIRS AEKKGLTVSL LSGNVIPVVY ALKIFLGING 

        70         80         90        100        110        120 
PVFGENGGIM FDNDGSIKKF FSNEGTNKFL EEMSKRTSMR SILTNRWREA STGFDIDPED 

       130        140        150        160        170        180 
VDYVRKEAES RGFVIFYSGY SWHLMNRGED KAFAVNKLKE MYSLEYDEIL VIGDSNNDMP 

       190        200        210        220 
MFQLPVRKAC PANATDNIKA VSDFVSDYSY GEEIGQIFKH FELM

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed: 11029001] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
[2]"Structure- and function-based characterization of a new phosphoglycolate phosphatase from Thermoplasma acidophilum."
Kim Y., Yakunin A.F., Kuznetsova E., Xu X., Pennycooke M., Gu J., Cheung F., Proudfoot M., Arrowsmith C.H., Joachimiak A., Edwards A.M., Christendat D.
J. Biol. Chem. 279:517-526(2004) [PubMed: 14555659] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS), FUNCTION, COFACTOR, KINETIC PARAMETERS, SUBUNIT.
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL445063 Genomic DNA. Translation: CAC11321.1.
RefSeqNP_393653.1. NC_002578.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KYTX-ray1.70A/B1-224[»]
1L6RX-ray1.40A/B1-224[»]
ProteinModelPortalQ9HLQ2.
SMRQ9HLQ2. Positions 1-224.
ModBaseSearch...

Proteomic databases

PRIDEQ9HLQ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1455819.
GenomeReviewsGene locus Ta0175 in contig AL139299_GR.
KEGGtac:Ta0175.
NMPDRfig|273075.1.peg.175.

Phylogenomic databases

HOGENOMHBG731500.
OMAVTGNTVQ.
PhylomeDBQ9HLQ2.
ProtClustDBPRK01158.

Enzyme and pathway databases

BioCycTACI273075:TA0175-MONOMER.
BRENDA3.1.3.18. 6324.

Family and domain databases

HAMAPMF_01419. GPH_hydrolase_arch.
[Tree]
InterProIPR023214. HAD-like_dom.
IPR013200. HAD-SF_hydro-like_3.
IPR006382. SPPlik_hydro_arc.
IPR006378. Suc_phosP.
[Graphical view]
Gene3DG3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KOK07024.
PfamPF08282. Hydrolase_3. 2 hits.
[Graphical view]
SUPFAMSSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01487. SPP-like. 1 hit.
TIGR01482. SPP-subfamily. 1 hit.
ProtoNetSearch...

Entry information

Entry namePGP_THEAC
AccessionPrimary (citable) accession number: Q9HLQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2001
Last modified: December 14, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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