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P75792 (SUPH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Sugar phosphatase YbiV

EC=3.1.3.23
Gene names
Name:ybiV
Synonyms:supH
Ordered Locus Names:b0822, JW0806
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolysis of sugar phosphate to sugar and inorganic phosphate. Has a wide substrate specificity catalyzing the hydrolysis of ribose-5-phosphate, glucose-6-phosphate, fructose-1-phosphate, acetyl-phosphate, glycerol-1-phosphate, glycerol-2-phosphate, 2-deoxy-glucose-6-phosphate, mannose-6-phosphate and fructose-6-phosphate. Appears to have a low level of phosphotransferase activity using monophosphates as the phosphate donor. Ref.4 Ref.5 Ref.6

Catalytic activity

Sugar phosphate + H2O = sugar + phosphate. Ref.6

Cofactor

Magnesium. Can also use other divalent metal cations as manganese, cobalt and zinc. Ref.5

Subunit structure

Homodimer. Ref.6 Ref.7

Induction

Regulated by the cAMP receptor protein crp Potential.

Sequence similarities

Belongs to the HAD-like hydrolase superfamily. Cof family. SupH subfamily.

Biophysicochemical properties

Kinetic parameters:

Glucose-6-phosphate is also a good substrate with a relative activity of 62.5% versus the activity with ribose-5-phosphate.

KM=0.12 mM for imido-di-phosphate (in the presence of magnesium ion as cofactor and at pH 9) Ref.5 Ref.6

KM=1.4 mM for fructose-1-phosphate (in the presence of magnesium ion as cofactor and at pH 9)

KM=2.4 mM for ribose-5-phosphate (in the presence of magnesium ion as cofactor and at pH 9)

KM=3.1 mM for glucose-6-phosphate (in the presence of magnesium ion as cofactor and at pH 9)

KM=4.9 mM for acetyl-phosphate (in the presence of magnesium ion as cofactor and at pH 9)

KM=6 mM for ribose-5-phosphate (at pH 5.4)

KM=6 mM for glycerol-1-phosphate (at pH 5.4)

KM=4.5 mM for glycerol-2-phosphate (at pH 5.4)

Ontologies

Keywords
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdephosphorylation

Inferred from direct assay Ref.5. Source: GOC

   Molecular_functionmagnesium ion binding

Inferred from direct assay Ref.5. Source: UniProtKB

sugar-phosphatase activity

Inferred from direct assay Ref.5. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Sugar phosphatase YbiV
PRO_0000054421

Regions

Region44 – 452Phosphate binding

Sites

Active site91Nucleophile Potential
Metal binding91Magnesium
Metal binding111Magnesium; via carbonyl oxygen
Metal binding2151Magnesium
Metal binding2161Magnesium
Binding site101Phosphate; via amide nitrogen
Binding site1921Phosphate
Binding site2181Phosphate By similarity

Secondary structure

........................................................... 271
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P75792 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: F8733636B422A9A9

FASTA27130,413
        10         20         30         40         50         60 
MSVKVIVTDM DGTFLNDAKT YNQPRFMAQY QELKKRGIKF VVASGNQYYQ LISFFPELKD 

        70         80         90        100        110        120 
EISFVAENGA LVYEHGKQLF HGELTRHESR IVIGELLKDK QLNFVACGLQ SAYVSENAPE 

       130        140        150        160        170        180 
AFVALMAKHY HRLKPVKDYQ EIDDVLFKFS LNLPDEQIPL VIDKLHVALD GIMKPVTSGF 

       190        200        210        220        230        240 
GFIDLIIPGL HKANGISRLL KRWDLSPQNV VAIGDSGNDA EMLKMARYSF AMGNAAENIK 

       250        260        270 
QIARYATDDN NHEGALNVIQ AVLDNTSPFN S 

« Hide

References

« Hide 'large scale' references
[1]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Enzyme genomics: application of general enzymatic screens to discover new enzymes."
Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A., Arrowsmith C.H., Edwards A.M., Yakunin A.F.
FEMS Microbiol. Rev. 29:263-279(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A PHOSPHATASE.
[5]"Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family."
Kuznetsova E., Proudfoot M., Gonzalez C.F., Brown G., Omelchenko M.V., Borozan I., Carmel L., Wolf Y.I., Mori H., Savchenko A.V., Arrowsmith C.H., Koonin E.V., Edwards A.M., Yakunin A.F.
J. Biol. Chem. 281:36149-36161(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A PHOSPHATASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
[6]"Ybiv from Escherichia coli K12 is a HAD phosphatase."
Roberts A., Lee S.-Y., McCullagh E., Silversmith R.E., Wemmer D.E.
Proteins 58:790-801(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PHOSPHATE ANALOGS AND MAGNESIUM ION, FUNCTION AS A PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT.
Strain: K12 / MG1655 / ATCC 47076.
[7]"Domain shifting confirms monomeric structure of Escherichia coli sugar phosphatase suph."
New York structural genomix research consortium (NYSGXRC)
Submitted (JUL-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-271, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC73909.1.
AP009048 Genomic DNA. Translation: BAA35503.1.
PIRF64819.
RefSeqNP_415343.1. NC_000913.3.
YP_489095.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RLMX-ray1.90A/B/C/D3-271[»]
1RLOX-ray2.00A/B/C/D3-271[»]
1RLTX-ray2.20A/B/C/D3-271[»]
2HF2X-ray1.90A/B2-271[»]
ProteinModelPortalP75792.
SMRP75792. Positions 1-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP75792. 10 interactions.
STRING511145.b0822.

Proteomic databases

PaxDbP75792.
PRIDEP75792.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73909; AAC73909; b0822.
BAA35503; BAA35503; BAA35503.
GeneID12934001.
945432.
KEGGecj:Y75_p0795.
eco:b0822.
PATRIC32116847. VBIEscCol129921_0849.

Organism-specific databases

EchoBASEEB3111.
EcoGeneEG13327. supH.

Phylogenomic databases

eggNOGCOG0561.
HOGENOMHOG000184782.
KOK07757.
OMATELEYYM.
OrthoDBEOG6H7FNB.
PhylomeDBP75792.
ProtClustDBCLSK879776.

Enzyme and pathway databases

BioCycEcoCyc:G6425-MONOMER.
ECOL316407:JW0806-MONOMER.
MetaCyc:G6425-MONOMER.

Gene expression databases

GenevestigatorP75792.

Family and domain databases

Gene3D3.40.50.1000. 2 hits.
InterProIPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR000150. Hypothet_cof.
[Graphical view]
PfamPF08282. Hydrolase_3. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR00099. Cof-subfamily. 1 hit.
TIGR01484. HAD-SF-IIB. 1 hit.
PROSITEPS01229. COF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP75792.
PROP75792.

Entry information

Entry nameSUPH_ECOLI
AccessionPrimary (citable) accession number: P75792
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene