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Protein

5'-nucleotidase SurE

Gene

surE

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Nucleotidase that preferentially dephosphorylates 5'-GMP and 5'-AMP.

Catalytic activityi

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

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit. In contrast to other surE homologs, is essentially inactive with other divalent cations.1 Publication

Enzyme regulationi

Inhibited by vanadate and tungstate.

Kineticsi

  1. KM=31.5 mM for pNPP (at 76 degrees Celsius)
  1. Vmax=51.6 µmol/min/mg enzyme with pNPP as substrate (at 76 degrees Celsius)

pH dependencei

Optimum pH is 5.5-6.2.

Temperature dependencei

Optimum temperature is 80 degrees Celsius. Active up to 95 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi8 – 81Magnesium
Metal bindingi9 – 91Magnesium
Metal bindingi39 – 391Magnesium
Metal bindingi95 – 951Magnesium

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
5'-nucleotidase SurE (EC:3.1.3.5)
Alternative name(s):
Nucleoside 5'-monophosphate phosphohydrolase
Gene namesi
Name:surE
Ordered Locus Names:TM_1662
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81D → N: Loss of activity. 1 Publication
Mutagenesisi9 – 91D → N: Loss of activity. 1 Publication
Mutagenesisi127 – 1271S → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2472475'-nucleotidase SurEPRO_0000111846Add
BLAST

Interactioni

Subunit structurei

Homodimer and possibly homotetramer.1 Publication

Protein-protein interaction databases

STRINGi243274.TM1662.

Structurei

Secondary structure

1
247
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi14 – 2310Combined sources
Turni24 – 263Combined sources
Beta strandi27 – 3610Combined sources
Beta strandi53 – 553Combined sources
Beta strandi59 – 6911Combined sources
Helixi71 – 8010Combined sources
Beta strandi88 – 9710Combined sources
Helixi101 – 1066Combined sources
Helixi108 – 11811Combined sources
Beta strandi123 – 1297Combined sources
Beta strandi131 – 1333Combined sources
Helixi136 – 14914Combined sources
Helixi152 – 1543Combined sources
Beta strandi160 – 1656Combined sources
Beta strandi172 – 1754Combined sources
Beta strandi182 – 19110Combined sources
Beta strandi197 – 20610Combined sources
Beta strandi212 – 2143Combined sources
Helixi215 – 2206Combined sources
Beta strandi223 – 2297Combined sources
Helixi236 – 24510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ILVX-ray2.00A/B1-247[»]
1J9JX-ray1.90A/B1-247[»]
1J9KX-ray2.10A/B1-247[»]
1J9LX-ray1.90A/B1-247[»]
ProteinModelPortaliP96112.
SMRiP96112. Positions 1-247.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP96112.

Family & Domainsi

Sequence similaritiesi

Belongs to the SurE nucleotidase family.Curated

Phylogenomic databases

eggNOGiENOG4105CV2. Bacteria.
COG0496. LUCA.
InParanoidiP96112.
KOiK03787.
OMAiNLNIPPC.
OrthoDBiEOG68WR45.

Family and domain databases

Gene3Di3.40.1210.10. 1 hit.
HAMAPiMF_00060. SurE.
InterProiIPR030048. SurE.
IPR002828. SurE-like_Pase/nucleotidase.
[Graphical view]
PfamiPF01975. SurE. 1 hit.
[Graphical view]
SUPFAMiSSF64167. SSF64167. 1 hit.
TIGRFAMsiTIGR00087. surE. 1 hit.

Sequencei

Sequence statusi: Complete.

P96112-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRILVTNDDG IQSKGIIVLA ELLSEEHEVF VVAPDKERSA TGHSITIHVP
60 70 80 90 100
LWMKKVFISE RVVAYSTTGT PADCVKLAYN VVMDKRVDLI VSGVNRGPNM
110 120 130 140 150
GMDILHSGTV SGAMEGAMMN IPSIAISSAN YESPDFEGAA RFLIDFLKEF
160 170 180 190 200
DFSLLDPFTM LNINVPAGEI KGWRFTRQSR RRWNDYFEER VSPFGEKYYW
210 220 230 240
MMGEVIEDDD RDDVDYKAVR EGYVSITPIH PFLTNEQCLK KLREVYD
Length:247
Mass (Da):28,075
Last modified:May 30, 2000 - v2
Checksum:i09F4A68A80C0B241
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36729.1.
Y10306 Genomic DNA. Translation: CAA71355.1.
PIRiD72224.
RefSeqiNP_229462.1. NC_000853.1.
WP_004082178.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD36729; AAD36729; TM_1662.
GeneIDi897339.
KEGGitma:TM1662.
PATRICi23938298. VBITheMar51294_1681.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36729.1.
Y10306 Genomic DNA. Translation: CAA71355.1.
PIRiD72224.
RefSeqiNP_229462.1. NC_000853.1.
WP_004082178.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ILVX-ray2.00A/B1-247[»]
1J9JX-ray1.90A/B1-247[»]
1J9KX-ray2.10A/B1-247[»]
1J9LX-ray1.90A/B1-247[»]
ProteinModelPortaliP96112.
SMRiP96112. Positions 1-247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1662.

Protocols and materials databases

DNASUi897339.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36729; AAD36729; TM_1662.
GeneIDi897339.
KEGGitma:TM1662.
PATRICi23938298. VBITheMar51294_1681.

Phylogenomic databases

eggNOGiENOG4105CV2. Bacteria.
COG0496. LUCA.
InParanoidiP96112.
KOiK03787.
OMAiNLNIPPC.
OrthoDBiEOG68WR45.

Miscellaneous databases

EvolutionaryTraceiP96112.

Family and domain databases

Gene3Di3.40.1210.10. 1 hit.
HAMAPiMF_00060. SurE.
InterProiIPR030048. SurE.
IPR002828. SurE-like_Pase/nucleotidase.
[Graphical view]
PfamiPF01975. SurE. 1 hit.
[Graphical view]
SUPFAMiSSF64167. SSF64167. 1 hit.
TIGRFAMsiTIGR00087. surE. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. "A survey of polypeptide deformylase function throughout the eubacterial lineage."
    Mazel D., Coic E., Blanchard S., Saurin W., Marliere P.
    J. Mol. Biol. 266:939-949(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 156-247.
  3. "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] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  4. "Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase."
    Zhang R.-G., Skarina T., Katz J.E., Beasley S., Khachatryan A., Vyas S., Arrowsmith C.H., Clarke S., Edwards A., Joachimiak A., Savchenko A.
    Structure 9:1095-1106(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), CHARACTERIZATION, SUBUNIT, MUTAGENESIS.
  5. "Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family."
    Lee J.Y., Kwak J.E., Moon J., Eom S.H., Liong E.C., Pedelacq J.-D., Berendzen J., Suh S.W.
    Nat. Struct. Biol. 8:789-794(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), CHARACTERIZATION.

Entry informationi

Entry nameiSURE_THEMA
AccessioniPrimary (citable) accession number: P96112
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: April 13, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.