P36136 (SHB17_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sedoheptulose 1,7-bisphosphatase
EC=3.1.3.37

Gene names

Name:	SHB17
Ordered Locus Names:	YKR043C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	271 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Ribosome biogenesis
Cellular component	Cytoplasm Nucleus
Molecular function	Hydrolase Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW ribose phosphate biosynthetic process Inferred from direct assay Ref.6. Source: SGD ribosome biogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.3. Source: SGD nucleus Inferred from direct assay Ref.3. Source: SGD
Molecular_function	oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW sedoheptulose-bisphosphatase activity Inferred from direct assay Ref.6. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 271

271

Sedoheptulose 1,7-bisphosphatase

PRO_0000203211

Regions

Region

24 – 25

2

Substrate

Region

99 – 102

4

Substrate

Region

176 – 181

6

Substrate

Sites

Active site

13

1

Tele-phosphohistidine intermediate

Active site

176

1

Binding site

12

1

Substrate

Binding site

69

1

Substrate

Binding site

181

1

Substrate

Binding site

244

1

Substrate

Experimental info

Mutagenesis

12

1

R → A: Impairs catalytic activity. Ref.5

Mutagenesis

13

1

H → A: Impairs catalytic activity. Ref.5

Mutagenesis

16

1

T → A: Impairs catalytic activity. Ref.5

Mutagenesis

19

1

S → A: Leads to reduced substrate affinity. Ref.5

Mutagenesis

24

1

Y → A: Leads to low activity and reduced substrate affinity. Ref.5

Mutagenesis

65

1

S → A: Leads to low activity and reduced substrate affinity. Ref.5

Mutagenesis

69

1

R → A: Leads to reduced substrate affinity. Ref.5

Mutagenesis

99

1

E → A: Impairs catalytic activity. Ref.5

Mutagenesis

102

1

Y → A: Impairs catalytic activity. Ref.5

Mutagenesis

131

1

W → A: Leads to reduced substrate affinity. Ref.5

Mutagenesis

176

1

H → A: Impairs catalytic activity. Ref.5

Mutagenesis

178

1

H → A: Leads to low activity and reduced substrate affinity. Ref.5

Mutagenesis

181

1

R → A: Leads to reduced substrate affinity. Ref.5

Secondary structure

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271

Helix Strand Turn

Details...

Beta strand

7 – 12

6

Helix

17 – 21

5

Beta strand

26 – 28

3

Helix

34 – 48

15

Helix

49 – 51

3

Helix

56 – 58

3

Beta strand

59 – 64

6

Helix

68 – 77

10

Turn

78 – 80

3

Helix

83 – 87

5

Beta strand

89 – 93

5

Helix

95 – 97

3

Helix

103 – 105

3

Helix

110 – 119

10

Beta strand

124 – 126

3

Helix

130 – 133

4

Helix

141 – 164

24

Beta strand

170 – 175

6

Helix

177 – 187

11

Beta strand

191 – 195

5

Helix

199 – 202

4

Beta strand

219 – 223

5

Beta strand

237 – 243

7

Beta strand

249 – 253

5

Turn

254 – 257

4

Helix

262 – 264

3

Sequences

	Sequence		Length	Mass (Da)
	P36136 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: FF934DE2F5145C40	FASTA	271	31,022
	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

References

	« Hide 'large scale' referencesShow '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. , 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 96604 / S288c / FY1679.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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.

PIR

S38115.

RefSeq

NP_012969.1. NM_001179833.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3F3K	X-ray	1.75	A/B	1-263	[»]
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	[»]

ProteinModelPortal

P36136.

SMR

P36136. Positions 2-263.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4847N.

IntAct

P36136. 1 interaction.

MINT

MINT-567834.

STRING

4932.YKR043C.

Proteomic databases

PaxDb

P36136.

PeptideAtlas

P36136.

PRIDE

P36136.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YKR043C; YKR043C; YKR043C.

GeneID

853917.

KEGG

sce:YKR043C.

Organism-specific databases

CYGD

YKR043c.

SGD

S000001751. SHB17.

Phylogenomic databases

eggNOG

COG0406.

HOGENOM

HOG000221683.

KO

K15634.

OMA

DGCENGE.

OrthoDB

EOG4BCHX4.

Gene expression databases

Genevestigator

P36136.

GermOnline

YKR043C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR013078. His_Pase_superF_clade-1.
[Graphical view]

Pfam

PF00300. His_Phos_1. 1 hit.
[Graphical view]

SMART

SM00855. PGAM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P36136.

NextBio

975261.

Entry information

Entry name

SHB17_YEAST

Accession

Primary (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:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program