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P75792 (SUPH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 SupH
EC=3.1.3.23
Gene names
Name:supH
Synonyms:ybiV
Ordered Locus Names:b0822, JW0806
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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 fructose-1-P most efficiently, but it remains uncertain if this is the real substrate in vivo. Ref.4 Ref.5

Catalytic activity

Sugar phosphate + H2O = sugar + phosphate.

Cofactor

Magnesium.

Subunit structure

Monomer Probable.

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

KM=6 mM for ribose-5-P

KM=6 mM for glycerol-1-P

KM=4.5 mM for glycerol-2-P

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

sugar-phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Sugar phosphatase SupH
PRO_0000054421

Sites

Active site91Nucleophile
Metal binding91Magnesium
Metal binding111Magnesium
Metal binding2151Magnesium
Metal binding2161Magnesium
Binding site461Substrate Potential
Binding site681Substrate Potential
Binding site1301Substrate Potential
Binding site1501Substrate Potential
Binding site1781Substrate Potential
Binding site1841Substrate Potential

Secondary structure

1 ........................................................... 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: 8905232] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"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: 15657928] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF NATIVE PROTEIN AND OF COMPLEX WITH METALFLUORIDE, FUNCTION.
Strain: K12 / MG1655 / ATCC 47076.
[5]"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: 15808744] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U00096 Genomic DNA. Translation: AAC73909.1.
AP009048 Genomic DNA. Translation: BAA35503.1.
PIRF64819.
RefSeqNP_415343.1. NC_000913.2.

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...

Protein-protein interaction databases

DIPDIP-11441N.
IntActP75792. 10 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000000516; EBESCP00000000516; EBESCG00000000434.
EBESCT00000018415; EBESCP00000017706; EBESCG00000017469.
GeneID945432.
GenomeReviewsGene locus JW0806 in contig AP009048_GR.
Gene locus b0822 in contig U00096_GR.
KEGGecj:JW0806.
eco:b0822.
PATRIC32116847. VBIEscCol129921_0849.

Organism-specific databases

EchoBASEEB3111.
EcoGeneEG13327. supH.

Phylogenomic databases

eggNOGCOG0561.
GeneTreeEBGT00050000009623.
HOGENOMHBG728500.
OMAFELQEVE.
PhylomeDBP75792.
ProtClustDBCLSK879776.

Enzyme and pathway databases

BioCycEcoCyc:G6425-MONOMER.
MetaCyc:G6425-MONOMER.

Gene expression databases

GenevestigatorP75792.

Family and domain databases

InterProIPR023214. HAD-like_dom.
IPR013200. HAD-SF_hydro-like_3.
IPR006379. HAD-SF_hydro_IIB.
IPR000150. Hypothet_cof.
[Graphical view]
Gene3DG3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KOK07757.
PfamPF08282. Hydrolase_3. 1 hit.
[Graphical view]
SUPFAMSSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR00099. Cof-subfamily. 1 hit.
TIGR01484. HAD-SF-IIB. 1 hit.
PROSITEPS01228. COF_1. False negative.
PS01229. COF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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: January 25, 2012
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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