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Protein

Sedoheptulose 1,7-bisphosphatase

Gene

SHB17

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei12 – 121Substrate1 Publication
Active sitei13 – 131Tele-phosphohistidine intermediate1 Publication
Binding sitei69 – 691Substrate1 Publication
Active sitei99 – 991Proton donor/acceptor1 Publication
Sitei176 – 1761Transition state stabilizer1 Publication
Binding sitei181 – 1811Substrate1 Publication
Binding sitei244 – 2441Substrate1 Publication

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Oxidoreductase

Keywords - Biological processi

Carbohydrate 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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121R → A: Impairs catalytic activity. 1 Publication
Mutagenesisi13 – 131H → A: Impairs catalytic activity. 1 Publication
Mutagenesisi16 – 161T → A: Impairs catalytic activity. 1 Publication
Mutagenesisi19 – 191S → A: Leads to reduced substrate affinity. 1 Publication
Mutagenesisi24 – 241Y → A: Leads to low activity and reduced substrate affinity. 1 Publication
Mutagenesisi65 – 651S → A: Leads to low activity and reduced substrate affinity. 1 Publication
Mutagenesisi69 – 691R → A: Leads to reduced substrate affinity. 1 Publication
Mutagenesisi99 – 991E → A: Impairs catalytic activity. 1 Publication
Mutagenesisi102 – 1021Y → A: Impairs catalytic activity. 1 Publication
Mutagenesisi131 – 1311W → A: Leads to reduced substrate affinity. 1 Publication
Mutagenesisi176 – 1761H → A: Impairs catalytic activity. 1 Publication
Mutagenesisi178 – 1781H → A: Leads to low activity and reduced substrate affinity. 1 Publication
Mutagenesisi181 – 1811R → A: Leads to reduced substrate affinity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Sedoheptulose 1,7-bisphosphatasePRO_0000203211Add
BLAST

Proteomic databases

MaxQBiP36136.
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. 18 interactions.
DIPiDIP-4847N.
IntActiP36136. 1 interaction.
MINTiMINT-567834.

Structurei

Secondary structure

1
271
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 126Combined sources
Helixi17 – 215Combined sources
Beta strandi26 – 283Combined sources
Helixi34 – 4815Combined sources
Helixi49 – 513Combined sources
Helixi56 – 583Combined sources
Beta strandi59 – 646Combined sources
Helixi68 – 7710Combined sources
Turni78 – 803Combined sources
Helixi83 – 875Combined sources
Beta strandi89 – 935Combined sources
Helixi95 – 973Combined sources
Helixi103 – 1053Combined sources
Helixi110 – 11910Combined sources
Beta strandi124 – 1263Combined sources
Helixi130 – 1334Combined sources
Helixi141 – 16424Combined sources
Beta strandi170 – 1756Combined sources
Helixi177 – 18711Combined sources
Beta strandi191 – 1955Combined sources
Helixi199 – 2024Combined sources
Beta strandi219 – 2235Combined sources
Beta strandi237 – 2437Combined sources
Beta strandi249 – 2535Combined sources
Turni254 – 2574Combined sources
Helixi262 – 2643Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-263.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36136.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 252Substrate binding1 Publication
Regioni99 – 1024Substrate binding1 Publication

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000221683.
InParanoidiP36136.
KOiK15634.
OMAiDIMVFAH.
OrthoDBiEOG092C4OP1.

Family and domain databases

CDDicd07067. HP_PGM_like. 1 hit.
Gene3Di3.40.50.1240. 1 hit.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34175. 18 interactions.
DIPiDIP-4847N.
IntActiP36136. 1 interaction.
MINTiMINT-567834.

PTM databases

iPTMnetiP36136.

Proteomic databases

MaxQBiP36136.
PRIDEiP36136.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKR043C; YKR043C; YKR043C.
GeneIDi853917.
KEGGisce:YKR043C.

Organism-specific databases

EuPathDBiFungiDB:YKR043C.
SGDiS000001751. SHB17.

Phylogenomic databases

HOGENOMiHOG000221683.
InParanoidiP36136.
KOiK15634.
OMAiDIMVFAH.
OrthoDBiEOG092C4OP1.

Enzyme and pathway databases

BioCyciYEAST:G3O-32014-MONOMER.
BRENDAi3.1.3.11. 984.

Miscellaneous databases

EvolutionaryTraceiP36136.
PROiP36136.

Family and domain databases

CDDicd07067. HP_PGM_like. 1 hit.
Gene3Di3.40.50.1240. 1 hit.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSHB17_YEAST
AccessioniPrimary (citable) accession number: P36136
Secondary accession number(s): D6VXA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: September 7, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.