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P36136 (SHB17_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Sedoheptulose 1,7-bisphosphatase

EC=3.1.3.37
Gene names
Name:SHB17
Ordered Locus Names:YKR043C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

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

General annotation (Comments)

Function

Sedoheptulose 1,7-bisphosphatase involved in riboneogenesis. Dephosphorylates sedoheptulose 1,7-bisphosphate (SBP), which is converted via the non-oxidative pentose phosphate pathway to ribose-5-phosphate. Has a fructose 1,6-bisphosphatase activity in vitro, but this is probably not biologically relevant, since deletion does not affect fructose 1,6-biphosphate (FBP) levels. Ref.6

Catalytic activity

Sedoheptulose 1,7-bisphosphate + H2O = sedoheptulose 7-phosphate + phosphate. Ref.5 Ref.6

Subunit structure

Homodimer. Ref.5 Ref.6

Subcellular location

Cytoplasm. Nucleus Ref.3.

Induction

Expression is correlated with levels of ribosomal proteins, thus periodic SHB17 expression coincides with the peak demand for ribose phosphate that occurs during ribosome synthesis. Ref.6

Miscellaneous

Present with 11500 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the phosphoglycerate mutase family. SHB17 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=34 µM for sedoheptulose 1,7-bisphosphate (SBP) Ref.5 Ref.6

KM=0.2 mM for fructose 1,6-bisphosphate (FBP)

KM=0.7 mM for fructose 1,6-bisphosphate (in the presence of 1 mM fructose 2,6-bisphosphate)

KM=2.3 mM for fructose 1,6-bisphosphate (in the presence of 2 mM fructose 2,6-bisphosphate)

KM=1.4 mM for fructose 1-phosphate

KM=1.6 mM for glyceraldehyde 3-phosphate

KM=0.3 mM for erythrose 4-phosphate

Vmax=7.8 µmol/min/mg enzyme toward sedoheptulose 1,7-bisphosphate (SBP)

Vmax=8.7 µmol/min/mg enzyme toward fructose 1,6-bisphosphate (FBP)

Vmax=7.3 µmol/min/mg enzyme toward fructose 1,6-bisphosphate (in the presence of 1 mM fructose 2,6-bisphosphate)

Vmax=8.9 µmol/min/mg enzyme toward fructose 1,6-bisphosphate,(in the presence of 1 mM fructose 2,6-bisphosphate)

Vmax=7.3 µmol/min/mg enzyme toward fructose 1-phosphate

Vmax=1 µmol/min/mg enzyme toward glyceraldehyde 3-phosphate

Vmax=0.6 µmol/min/mg enzyme toward erythrose 4-phosphate

pH dependence:

Optimum pH is 6.5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 271271Sedoheptulose 1,7-bisphosphatase
PRO_0000203211

Regions

Region24 – 252Substrate binding
Region99 – 1024Substrate binding

Sites

Active site131Tele-phosphohistidine intermediate
Active site1761
Binding site121Substrate
Binding site691Substrate
Binding site1811Substrate
Binding site2441Substrate

Experimental info

Mutagenesis121R → A: Impairs catalytic activity. Ref.5
Mutagenesis131H → A: Impairs catalytic activity. Ref.5
Mutagenesis161T → A: Impairs catalytic activity. Ref.5
Mutagenesis191S → A: Leads to reduced substrate affinity. Ref.5
Mutagenesis241Y → A: Leads to low activity and reduced substrate affinity. Ref.5
Mutagenesis651S → A: Leads to low activity and reduced substrate affinity. Ref.5
Mutagenesis691R → A: Leads to reduced substrate affinity. Ref.5
Mutagenesis991E → A: Impairs catalytic activity. Ref.5
Mutagenesis1021Y → A: Impairs catalytic activity. Ref.5
Mutagenesis1311W → A: Leads to reduced substrate affinity. Ref.5
Mutagenesis1761H → A: Impairs catalytic activity. Ref.5
Mutagenesis1781H → A: Leads to low activity and reduced substrate affinity. Ref.5
Mutagenesis1811R → A: Leads to reduced substrate affinity. Ref.5

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P36136 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: FF934DE2F5145C40

FASTA27131,022
        10         20         30         40         50         60 
MPSLTPRCII VRHGQTEWSK SGQYTGLTDL PLTPYGEGQM LRTGESVFRN NQFLNPDNIT 

        70         80         90        100        110        120 
YIFTSPRLRA RQTVDLVLKP LSDEQRAKIR VVVDDDLREW EYGDYEGMLT REIIELRKSR 

       130        140        150        160        170        180 
GLDKERPWNI WRDGCENGET TQQIGLRLSR AIARIQNLHR KHQSEGRASD IMVFAHGHAL 

       190        200        210        220        230        240 
RYFAAIWFGL GVQKKCETIE EIQNVKSYDD DTVPYVKLES YRHLVDNPCF LLDAGGIGVL 

       250        260        270 
SYAHHNIDEP ALELAGPFVS PPEEESQHGD V 

« Hide

References

« Hide 'large scale' references
[1]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"Structure and activity of the metal-independent fructose-1,6-bisphosphatase YK23 from Saccharomyces cerevisiae."
Kuznetsova E., Xu L., Singer A., Brown G., Dong A., Flick R., Cui H., Cuff M., Joachimiak A., Savchenko A., Yakunin A.F.
J. Biol. Chem. 285:21049-21059(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH FBP, SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-12; HIS-13; THR-16; SER-19; TYR-24; SER-65; ARG-69; GLU-99; TYR-102; TRP-131; HIS-176; HIS-178 AND ARG-181.
[6]"Riboneogenesis in yeast."
Clasquin M.F., Melamud E., Singer A., Gooding J.R., Xu X., Dong A., Cui H., Campagna S.R., Savchenko A., Yakunin A.F., Rabinowitz J.D., Caudy A.A.
Cell 145:969-980(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH SBP, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z28268 Genomic DNA. Translation: CAA82119.1.
BK006944 Genomic DNA. Translation: DAA09195.1.
PIRS38115.
RefSeqNP_012969.1. NM_001179833.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3F3KX-ray1.75A/B2-263[»]
3LG2X-ray2.60A/B/C/D1-271[»]
3LL4X-ray2.49A/B1-271[»]
3OI7X-ray2.40A/B/C/D1-271[»]
ProteinModelPortalP36136.
SMRP36136. Positions 2-263.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34175. 19 interactions.
DIPDIP-4847N.
IntActP36136. 1 interaction.
MINTMINT-567834.
STRING4932.YKR043C.

Proteomic databases

MaxQBP36136.
PaxDbP36136.
PeptideAtlasP36136.
PRIDEP36136.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKR043C; YKR043C; YKR043C.
GeneID853917.
KEGGsce:YKR043C.

Organism-specific databases

CYGDYKR043c.
SGDS000001751. SHB17.

Phylogenomic databases

eggNOGCOG0406.
HOGENOMHOG000221683.
KOK15634.
OMAGCENGES.
OrthoDBEOG7N9068.

Enzyme and pathway databases

BioCycYEAST:G3O-32014-MONOMER.

Gene expression databases

GenevestigatorP36136.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
InterProIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMSSF53254. SSF53254. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP36136.
NextBio975261.

Entry information

Entry nameSHB17_YEAST
AccessionPrimary (citable) accession number: P36136
Secondary accession number(s): D6VXA5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references