NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
PubMed=12125824 [NCBI, ExPASy, EBI, Israel, Japan]
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.;
"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.";
J. Mol. Microbiol. Biotechnol. 4:453-461(2002).

Comments

FUNCTION: Catalyzes the dephosphorylation of 2-phosphoglycolate (By similarity).
CATALYTIC ACTIVITY: 2-phosphoglycolate + H₂O = glycolate + phosphate.
COFACTOR: Magnesium (By similarity).
SIMILARITY: Belongs to the archaeal SPP-like hydrolase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE008384; AAM30152.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_632480.1; -.

3D structure databases

ModBase

Q8PZN6.

Enzyme and pathway databases

BioCyc

MMAZ192952:MM0456-MON; -.

Ontologies

GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008967;	Molecular function: phosphoglycolate phosphatase activity (inferred from electronic annotation from HAMAP).
GO:0005975;	Biological process: carbohydrate metabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01419; -; 1.
PBIL [Tree]

InterPro

IPR013200; HAD-SF_hydro-like_3.
IPR006379; HAD-SF_hydro_IIB.
IPR006382; SPPlik_hydro_arc.
IPR006378; Suc_phosP.
Graphical view of domain structure.

Pfam

PF08282; Hydrolase_3; 2.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01484; HAD-SF-IIB; 1.
TIGR01487; SPP-like; 1.
TIGR01482; SPP-subfamily; 1.

ProtoNet

Q8PZN6.

Genome annotation databases

GeneID

1478798; -.

GenomeReviews

AE008384_GR; MM_0456.

KEGG

mma:MM_0456; -.

NMPDR

fig|192952.1.peg.456; -.

Phylogenomic databases

HOGENOM

Q8PZN6; -.

Genome annotation databases

CMR

Q8PZN6; MM_0456.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Carbohydrate metabolism; Complete proteome; Hydrolase; Magnesium; Metal-binding.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 226`	`226`	`Phosphoglycolate phosphatase.`	`PRO_0000146719`
`ACT_SITE`	`9 9`		`Nucleophile (By similarity).`
`METAL`	`9 9`		`Magnesium (By similarity).`
`METAL`	`11 11`		`Magnesium (By similarity).`
`METAL`	`173 173`		`Magnesium (By similarity).`
`METAL`	`177 177`		`Magnesium (By similarity).`
`BINDING`	`150 150`		`Substrate (By similarity).`

Sequence information

Length: 226 AA [This is the length of the unprocessed precursor]

Molecular weight: 24677 Da [This is the MW of the unprocessed precursor]

CRC64: 9ED4C75961057A5D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKFKALVIDI DGTITCKNRE LHLGAVKKMR TLNVPVVLAT GNILCYARTA SRLIGLGGAV 

        70         80         90        100        110        120 
IAENGGAVTV RYDVNGIFEG SLEECEKAFS FLSQHFKLTK LDPTYRKTEI ALRRDFDLEE 

       130        140        150        160        170        180 
ARSLLETQPF DIELVDTKYA IHIKSIKINK GIGLQKLAGM MGFEAEDFVA IGDSANDAEM 

       190        200        210        220 
FEAAGFGIAV ANGDERVKEV ANYVTEASFG DGAVEAIEFL ESNGWI

Q8PZN6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools