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Protein

5'/3'-nucleotidase SurE

Gene

surE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. Also plays a significant physiological role in stress-response and is required for the survival of E.coli in stationary growth phase.1 Publication

Catalytic activityi

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
A 3'-ribonucleotide + H2O = a ribonucleoside + phosphate.
(Polyphosphate)(n) + H2O = (polyphosphate)(n-1) + phosphate.

Cofactori

Mn2+1 Publication, Co2+1 Publication, Ni2+1 Publication, Mg2+1 Publication, Zn2+1 PublicationNote: Binds 1 divalent metal cation per subunit. Highest nucleotidase activity with Mn2+, followed by Co2+, Ni2+ and Mg2+. Highest exopolyphosphatase activity with Mg2+, followed by Co2+ and Zn2+.1 Publication

Enzyme regulationi

Inhibited by various ribo- or deoxyribonucleoside 5'-triphosphates but is insensitive to nucleoside diphosphates.

Kineticsi

  1. KM=0.32 mM for 5'-AMP1 Publication
  2. KM=0.26 mM for 5'-GMP1 Publication
  3. KM=0.28 mM for 5'-dGMP1 Publication
  4. KM=0.10 mM for 3'-AMP1 Publication
  5. KM=0.37 mM for 3'-CMP1 Publication
  6. KM=2.49 mM for pNPP1 Publication
  7. KM=0.02 mM for polyphosphate1 Publication
  1. Vmax=10.0 µmol/min/mg enzyme with 5'-AMP as substrate1 Publication
  2. Vmax=22.4 µmol/min/mg enzyme with 5'-GMP as substrate1 Publication
  3. Vmax=16.4 µmol/min/mg enzyme with 5'-dGMP as substrate1 Publication
  4. Vmax=20.1 µmol/min/mg enzyme with 3'-AMP as substrate1 Publication
  5. Vmax=12.1 µmol/min/mg enzyme with 3'-CMP as substrate1 Publication
  6. Vmax=7.24 µmol/min/mg enzyme with pNPP as substrate1 Publication
  7. Vmax=0.10 µmol/min/mg enzyme with polyphosphate as substrate1 Publication

pH dependencei

Optimum pH is 7.0-7.2 for nucleotidase activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi8Divalent metal cationBy similarity1
Metal bindingi9Divalent metal cationBy similarity1
Metal bindingi39Divalent metal cationBy similarity1
Metal bindingi92Divalent metal cationBy similarity1

GO - Molecular functioni

  • 3'-nucleotidase activity Source: EcoCyc
  • 5'-nucleotidase activity Source: EcoCyc
  • exopolyphosphatase activity Source: EcoCyc
  • manganese ion binding Source: EcoCyc
  • nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  • UMP catabolic process Source: EcoCyc

Keywordsi

Molecular functionHydrolase
LigandCobalt, Magnesium, Manganese, Metal-binding, Nickel, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG11817-MONOMER.
MetaCyc:EG11817-MONOMER.
BRENDAi3.1.3.5. 2026.
3.1.3.6. 2026.
3.6.1.11. 2026.
SABIO-RKiP0A840.

Names & Taxonomyi

Protein namesi
Recommended name:
5'/3'-nucleotidase SurE (EC:3.1.3.5, EC:3.1.3.6)
Alternative name(s):
Exopolyphosphatase (EC:3.6.1.11)
Nucleoside monophosphate phosphohydrolase
Stationary-phase survival protein SurE
Gene namesi
Name:surE
Synonyms:ygbC
Ordered Locus Names:b2744, JW2714
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11817. surE.

Subcellular locationi

P0A840:

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001118091 – 2535'/3'-nucleotidase SurEAdd BLAST253

Proteomic databases

PaxDbiP0A840.
PRIDEiP0A840.

Interactioni

Subunit structurei

Monomer and homooligomer in solution. The oligomeric complex consists of at least four subunits.1 Publication

Protein-protein interaction databases

BioGridi4262277. 12 interactors.
DIPiDIP-47982N.
IntActiP0A840. 3 interactors.
STRINGi316385.ECDH10B_2912.

Structurei

3D structure databases

ProteinModelPortaliP0A840.
SMRiP0A840.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SurE nucleotidase family.Curated

Phylogenomic databases

eggNOGiENOG4105CV2. Bacteria.
COG0496. LUCA.
HOGENOMiHOG000122500.
InParanoidiP0A840.
KOiK03787.
PhylomeDBiP0A840.

Family and domain databases

Gene3Di3.40.1210.10. 1 hit.
HAMAPiMF_00060. SurE. 1 hit.
InterProiView protein in InterPro
IPR030048. SurE.
IPR002828. SurE-like_Pase/nucleotidase.
IPR036523. SurE-like_sf.
PfamiView protein in Pfam
PF01975. SurE. 1 hit.
SUPFAMiSSF64167. SSF64167. 1 hit.
TIGRFAMsiTIGR00087. surE. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A840-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRILLSNDDG VHAPGIQTLA KALREFADVQ VVAPDRNRSG ASNSLTLESS
60 70 80 90 100
LRTFTFENGD IAVQMGTPTD CVYLGVNALM RPRPDIVVSG INAGPNLGDD
110 120 130 140 150
VIYSGTVAAA MEGRHLGFPA LAVSLDGHKH YDTAAAVTCS ILRALCKEPL
160 170 180 190 200
RTGRILNINV PDLPLDQIKG IRVTRCGTRH PADQVIPQQD PRGNTLYWIG
210 220 230 240 250
PPGGKCDAGP GTDFAAVDEG YVSITPLHVD LTAHSAQDVV SDWLNSVGVG

TQW
Length:253
Mass (Da):26,900
Last modified:June 7, 2005 - v1
Checksum:i33A7CD0AEE13C3DB
GO

Sequence cautioni

P0A840: The sequence AAA69254 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07942 Genomic DNA. Translation: AAA79839.1.
U29579 Genomic DNA. Translation: AAA69254.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75786.1.
AP009048 Genomic DNA. Translation: BAE76821.1.
PIRiI69732.
RefSeqiNP_417224.1. NC_000913.3.
WP_001295182.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75786; AAC75786; b2744.
BAE76821; BAE76821; BAE76821.
GeneIDi947211.
KEGGiecj:JW2714.
eco:b2744.
PATRICifig|511145.12.peg.2839.

Similar proteinsi

Entry informationi

Entry nameiSURE_ECOLI
AccessioniPrimary (citable) accession number: P0A840
Secondary accession number(s): P36664, Q2MA85
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: October 25, 2017
This is version 97 of the entry and version 1 of the sequence. See 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

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families