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Q8ZU79 (SURE1_PYRAE) 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5'-nucleotidase surE1

EC=3.1.3.5
Alternative name(s):
Nucleoside 5'-monophosphate phosphohydrolase 1
Gene names
Name:surE1
Ordered Locus Names:PAE2908
OrganismPyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Taxonomic identifier178306 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Nucleotidase that shows the greatest phosphatase activity on purine (deoxy)nucleoside 5'-monophosphates, particularly the substrates 5'-GMP, 5'-AMP and 2'-deoxy-5'-AMP. Ref.2

Catalytic activity

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. HAMAP MF_00060

Cofactor

Binds 1 divalent metal cation per subunit. Most active with Co2+, and may utilize Mg2+ or Mn2+, though with less activity. Ref.2

Subunit structure

Homodimer. Ref.2

Subcellular location

Cytoplasm Potential HAMAP MF_00060.

Sequence similarities

Belongs to the surE nucleotidase family.

Caution

Was originally annotated as an acid phosphatase (EC 3.1.3.2).

Biophysicochemical properties

Temperature dependence:

Optimum temperature is above 90 degrees Celsius. HAMAP MF_00060

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCobalt
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function5'-nucleotidase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2662665'-nucleotidase surE1 HAMAP MF_00060
PRO_0000111869

Sites

Metal binding81Divalent metal cation By similarity
Metal binding91Divalent metal cation By similarity
Metal binding391Divalent metal cation By similarity
Metal binding931Divalent metal cation By similarity

Secondary structure

......................................... 266
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8ZU79 [UniParc].

Last modified March 5, 2002. Version 1.
Checksum: 292677D5D59149D0

FASTA26628,845
        10         20         30         40         50         60 
MKILVTNDDG VHSPGLRLLY QFALSLGDVD VVAPESPKSA TGLGITLHKP LRMYEVDLCG 

        70         80         90        100        110        120 
FRAIATSGTP SDTVYLATFG LGRKYDIVLS GINLGDNTSL QVILSSGTLG AAFQAALLGI 

       130        140        150        160        170        180 
PALAYSAYLE NWNELLNNKE AVEIMGAVVS STASYVLKNG MPQGVDVISV NFPRRLGRGV 

       190        200        210        220        230        240 
RAKLVKAAKL RYAQQVVERV DPRGVRYYWL YGRDLAPEPE TDVYVVLKEG GIAITPLTLN 

       250        260 
LNAVDAHREV DMDSLNRMVE YINASL 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum."
Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., Miller J.H.
Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002) [PubMed: 11792869] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827.
[2]"Structure and function of an archaeal homolog of survival protein E (SurEalpha): an acid phosphatase with purine nucleotide specificity."
Mura C., Katz J.E., Clarke S.G., Eisenberg D.
J. Mol. Biol. 326:1559-1575(2003) [PubMed: 12595266] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, CHARACTERIZATION, COFACTOR, SUBUNIT, TEMPERATURE DEPENDENCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009441 Genomic DNA. Translation: AAL64529.1.
RefSeqNP_560347.1. NC_003364.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1L5XX-ray2.00A/B1-266[»]
ProteinModelPortalQ8ZU79.
SMRQ8ZU79. Positions 1-266.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1463691.
GenomeReviewsGene locus PAE2908 in contig AE009441_GR.
KEGGpai:PAE2908.
NMPDRfig|178306.1.peg.2037.

Phylogenomic databases

HOGENOMHBG600532.
OMAHAPALIR.
ProtClustDBPRK13934.

Enzyme and pathway databases

BioCycPAER178306:PAE2908-MONOMER.

Family and domain databases

HAMAPMF_00060. SurE.
[Tree]
InterProIPR002828. SurE-like_Pase/nucleotidase.
[Graphical view]
Gene3DG3DSA:3.40.1210.10. SurE-like_Pase/nucleotidase. 1 hit.
KOK03787.
PfamPF01975. SurE. 1 hit.
[Graphical view]
SUPFAMSSF64167. SurE-like_Pase/nucleotidase. 1 hit.
TIGRFAMsTIGR00087. SurE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSURE1_PYRAE
AccessionPrimary (citable) accession number: Q8ZU79
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
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