Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Sedoheptulose 1,7-bisphosphatase

Gene

SHB17

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.1 Publication

Miscellaneous

Present with 11500 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

Sedoheptulose 1,7-bisphosphate + H2O = sedoheptulose 7-phosphate + phosphate.2 Publications

Kineticsi

  1. KM=34 µM for sedoheptulose 1,7-bisphosphate (SBP)2 Publications
  2. KM=0.2 mM for fructose 1,6-bisphosphate (FBP)2 Publications
  3. KM=0.7 mM for fructose 1,6-bisphosphate (in the presence of 1 mM fructose 2,6-bisphosphate)2 Publications
  4. KM=2.3 mM for fructose 1,6-bisphosphate (in the presence of 2 mM fructose 2,6-bisphosphate)2 Publications
  5. KM=1.4 mM for fructose 1-phosphate2 Publications
  6. KM=1.6 mM for glyceraldehyde 3-phosphate2 Publications
  7. KM=0.3 mM for erythrose 4-phosphate2 Publications
  1. Vmax=7.8 µmol/min/mg enzyme toward sedoheptulose 1,7-bisphosphate (SBP)2 Publications
  2. Vmax=8.7 µmol/min/mg enzyme toward fructose 1,6-bisphosphate (FBP)2 Publications
  3. Vmax=7.3 µmol/min/mg enzyme toward fructose 1,6-bisphosphate (in the presence of 1 mM fructose 2,6-bisphosphate)2 Publications
  4. Vmax=8.9 µmol/min/mg enzyme toward fructose 1,6-bisphosphate,(in the presence of 1 mM fructose 2,6-bisphosphate)2 Publications
  5. Vmax=7.3 µmol/min/mg enzyme toward fructose 1-phosphate2 Publications
  6. Vmax=1 µmol/min/mg enzyme toward glyceraldehyde 3-phosphate2 Publications
  7. Vmax=0.6 µmol/min/mg enzyme toward erythrose 4-phosphate2 Publications

pH dependencei

Optimum pH is 6.5.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei12Substrate1 Publication1
Active sitei13Tele-phosphohistidine intermediate1 Publication1
Binding sitei69Substrate1 Publication1
Active sitei99Proton donor/acceptor1 Publication1
Sitei176Transition state stabilizer1 Publication1
Binding sitei181Substrate1 Publication1
Binding sitei244Substrate1 Publication1

GO - Molecular functioni

  • oxidoreductase activity Source: UniProtKB-KW
  • sedoheptulose-bisphosphatase activity Source: SGD

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Oxidoreductase
Biological processCarbohydrate metabolism, Ribosome biogenesis

Enzyme and pathway databases

BioCyciYEAST:G3O-32014-MONOMER
BRENDAi3.1.3.11 984

Names & Taxonomyi

Protein namesi
Recommended name:
Sedoheptulose 1,7-bisphosphatase (EC:3.1.3.37)
Gene namesi
Name:SHB17
Ordered Locus Names:YKR043C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKR043C
SGDiS000001751 SHB17

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi12R → A: Impairs catalytic activity. 1 Publication1
Mutagenesisi13H → A: Impairs catalytic activity. 1 Publication1
Mutagenesisi16T → A: Impairs catalytic activity. 1 Publication1
Mutagenesisi19S → A: Leads to reduced substrate affinity. 1 Publication1
Mutagenesisi24Y → A: Leads to low activity and reduced substrate affinity. 1 Publication1
Mutagenesisi65S → A: Leads to low activity and reduced substrate affinity. 1 Publication1
Mutagenesisi69R → A: Leads to reduced substrate affinity. 1 Publication1
Mutagenesisi99E → A: Impairs catalytic activity. 1 Publication1
Mutagenesisi102Y → A: Impairs catalytic activity. 1 Publication1
Mutagenesisi131W → A: Leads to reduced substrate affinity. 1 Publication1
Mutagenesisi176H → A: Impairs catalytic activity. 1 Publication1
Mutagenesisi178H → A: Leads to low activity and reduced substrate affinity. 1 Publication1
Mutagenesisi181R → A: Leads to reduced substrate affinity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002032111 – 271Sedoheptulose 1,7-bisphosphataseAdd BLAST271

Proteomic databases

MaxQBiP36136
PaxDbiP36136
PRIDEiP36136

PTM databases

iPTMnetiP36136

Expressioni

Inductioni

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.1 Publication

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi34175, 102 interactors
DIPiDIP-4847N
IntActiP36136, 1 interactor
MINTiP36136
STRINGi4932.YKR043C

Structurei

Secondary structure

1271
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 12Combined sources6
Helixi17 – 21Combined sources5
Beta strandi26 – 28Combined sources3
Helixi34 – 48Combined sources15
Helixi49 – 51Combined sources3
Helixi56 – 58Combined sources3
Beta strandi59 – 64Combined sources6
Helixi68 – 77Combined sources10
Turni78 – 80Combined sources3
Helixi83 – 87Combined sources5
Beta strandi89 – 93Combined sources5
Helixi95 – 97Combined sources3
Helixi103 – 105Combined sources3
Helixi110 – 119Combined sources10
Beta strandi124 – 126Combined sources3
Helixi130 – 133Combined sources4
Helixi141 – 164Combined sources24
Beta strandi170 – 175Combined sources6
Helixi177 – 187Combined sources11
Beta strandi191 – 195Combined sources5
Helixi199 – 202Combined sources4
Beta strandi219 – 223Combined sources5
Beta strandi237 – 243Combined sources7
Beta strandi249 – 253Combined sources5
Turni254 – 257Combined sources4
Helixi262 – 264Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP36136
SMRiP36136
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36136

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni24 – 25Substrate binding1 Publication2
Regioni99 – 102Substrate binding1 Publication4

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000221683
InParanoidiP36136
KOiK22315
OMAiVCGFEHG
OrthoDBiEOG092C4OP1

Family and domain databases

CDDicd07067 HP_PGM_like, 1 hit
Gene3Di3.40.50.1240, 1 hit
InterProiView protein in InterPro
IPR013078 His_Pase_superF_clade-1
IPR029033 His_PPase_superfam
PfamiView protein in Pfam
PF00300 His_Phos_1, 1 hit
SMARTiView protein in SMART
SM00855 PGAM, 1 hit
SUPFAMiSSF53254 SSF53254, 1 hit

Sequencei

Sequence statusi: Complete.

P36136-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSLTPRCII VRHGQTEWSK SGQYTGLTDL PLTPYGEGQM LRTGESVFRN
60 70 80 90 100
NQFLNPDNIT YIFTSPRLRA RQTVDLVLKP LSDEQRAKIR VVVDDDLREW
110 120 130 140 150
EYGDYEGMLT REIIELRKSR GLDKERPWNI WRDGCENGET TQQIGLRLSR
160 170 180 190 200
AIARIQNLHR KHQSEGRASD IMVFAHGHAL RYFAAIWFGL GVQKKCETIE
210 220 230 240 250
EIQNVKSYDD DTVPYVKLES YRHLVDNPCF LLDAGGIGVL SYAHHNIDEP
260 270
ALELAGPFVS PPEEESQHGD V
Length:271
Mass (Da):31,022
Last modified:June 1, 1994 - v1
Checksum:iFF934DE2F5145C40
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28268 Genomic DNA Translation: CAA82119.1
BK006944 Genomic DNA Translation: DAA09195.1
PIRiS38115
RefSeqiNP_012969.1, NM_001179833.1

Genome annotation databases

EnsemblFungiiYKR043C; YKR043C; YKR043C
GeneIDi853917
KEGGisce:YKR043C

Similar proteinsi

Entry informationi

Entry nameiSHB17_YEAST
AccessioniPrimary (citable) accession number: P36136
Secondary accession number(s): D6VXA5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 23, 2018
This is version 127 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health