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P36136

- SHB17_YEAST

UniProt

P36136 - SHB17_YEAST

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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: 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

Vmax=7.8 µmol/min/mg enzyme toward sedoheptulose 1,7-bisphosphate (SBP)2 Publications

Vmax=8.7 µmol/min/mg enzyme toward fructose 1,6-bisphosphate (FBP)2 Publications

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

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

Vmax=7.3 µmol/min/mg enzyme toward fructose 1-phosphate2 Publications

Vmax=1 µmol/min/mg enzyme toward glyceraldehyde 3-phosphate2 Publications

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 – 121Substrate
Active sitei13 – 131Tele-phosphohistidine intermediate
Binding sitei69 – 691Substrate
Active sitei176 – 1761
Binding sitei181 – 1811Substrate
Binding sitei244 – 2441Substrate

GO - Molecular functioni

  1. oxidoreductase activity Source: UniProtKB-KW
  2. sedoheptulose-bisphosphatase activity Source: SGD

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
  2. dephosphorylation Source: GOC
  3. ribose phosphate biosynthetic process Source: SGD
  4. ribosome biogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Ribosome biogenesis

Enzyme and pathway databases

BioCyciYEAST:G3O-32014-MONOMER.

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
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

CYGDiYKR043c.
SGDiS000001751. SHB17.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
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.
PaxDbiP36136.
PeptideAtlasiP36136.
PRIDEiP36136.

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

Gene expression databases

GenevestigatoriP36136.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi34175. 20 interactions.
DIPiDIP-4847N.
IntActiP36136. 1 interaction.
MINTiMINT-567834.
STRINGi4932.YKR043C.

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 binding
Regioni99 – 1024Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0406.
HOGENOMiHOG000221683.
InParanoidiP36136.
KOiK15634.
OMAiGCENGES.
OrthoDBiEOG7N9068.

Family and domain databases

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 .
PIRi S38115.
RefSeqi NP_012969.1. NM_001179833.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3F3K X-ray 1.75 A/B 2-263 [» ]
3LG2 X-ray 2.60 A/B/C/D 1-271 [» ]
3LL4 X-ray 2.49 A/B 1-271 [» ]
3OI7 X-ray 2.40 A/B/C/D 1-271 [» ]
ProteinModelPortali P36136.
SMRi P36136. Positions 2-263.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34175. 20 interactions.
DIPi DIP-4847N.
IntActi P36136. 1 interaction.
MINTi MINT-567834.
STRINGi 4932.YKR043C.

Proteomic databases

MaxQBi P36136.
PaxDbi P36136.
PeptideAtlasi P36136.
PRIDEi P36136.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKR043C ; YKR043C ; YKR043C .
GeneIDi 853917.
KEGGi sce:YKR043C.

Organism-specific databases

CYGDi YKR043c.
SGDi S000001751. SHB17.

Phylogenomic databases

eggNOGi COG0406.
HOGENOMi HOG000221683.
InParanoidi P36136.
KOi K15634.
OMAi GCENGES.
OrthoDBi EOG7N9068.

Enzyme and pathway databases

BioCyci YEAST:G3O-32014-MONOMER.

Miscellaneous databases

EvolutionaryTracei P36136.
NextBioi 975261.

Gene expression databases

Genevestigatori P36136.

Family and domain databases

Gene3Di 3.40.50.1240. 1 hit.
InterProi IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
[Graphical view ]
Pfami PF00300. His_Phos_1. 1 hit.
[Graphical view ]
SMARTi SM00855. PGAM. 1 hit.
[Graphical view ]
SUPFAMi SSF53254. SSF53254. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH SBP, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.

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: November 26, 2014
This is version 100 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

External Data

Dasty 3