Fructose-1,6-bisphosphatase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P09201 (F16P_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 124. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Fructose-1,6-bisphosphatase
Short name=FBPase
EC=3.1.3.11

Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase

Gene names

Name:	FBP1
Ordered Locus Names:	YLR377C
ORF Names:	L8039.18

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-fructose 1,6-bisphosphate + H₂O = D-fructose 6-phosphate + phosphate.
Cofactor	Binds 3 magnesium ions per subunit By similarity.
Enzyme regulation	Subject to complex allosteric regulation. The enzyme can assume an active R-state, or an inactive T-state. Intermediate conformations may exist. AMP acts as allosteric inhibitor. AMP binding affects the turnover of bound substrate and not the affinity for substrate By similarity.
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
Subunit structure	Homotetramer By similarity.
Miscellaneous	Present with 589 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the FBPase class 1 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Inferred from mutant phenotype PubMed 6321183. Source: SGD reactive oxygen species metabolic process Inferred from mutant phenotype PubMed 16199065. Source: SGD
Cellular_component	cytosol Inferred from direct assay PubMed 12686616 PubMed 196563. Source: SGD
Molecular_function	fructose 1,6-bisphosphate 1-phosphatase activity Inferred from direct assay PubMed 6304022. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 348

347

Fructose-1,6-bisphosphatase

PRO_0000200511

Regions

Nucleotide binding

38 – 42

AMP By similarity

Nucleotide binding

122 – 123

AMP By similarity

Region

131 – 134

Substrate binding By similarity

Sites

Metal binding

Magnesium 1 By similarity

Metal binding

108

Magnesium 1 By similarity

Metal binding

108

Magnesium 2 By similarity

Metal binding

128

Magnesium 2 By similarity

Metal binding

128

Magnesium 3 By similarity

Metal binding

130

Magnesium 2; via carbonyl oxygen By similarity

Metal binding

131

Magnesium 3 By similarity

Metal binding

292

Magnesium 3 By similarity

Binding site

222

Substrate By similarity

Binding site

256

Substrate By similarity

Binding site

276

Substrate By similarity

Binding site

286

Substrate By similarity

Experimental info

Sequence conflict

278

C → D AA sequence Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P09201 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: BCFC0984A086094B
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FASTA

348

38,263

        10         20         30         40         50         60 
MPTLVNGPRR DSTEGFDTDI ITLPRFIIEH QKQFKNATGD FTLVLNALQF AFKFVSHTIR 

        70         80         90        100        110        120 
RAELVNLVGL AGASNFTGDQ QKKLDVLGDE IFINAMRASG IIKVLVSEEQ EDLIVFPTNT 

       130        140        150        160        170        180 
GSYAVCCDPI DGSSNLDAGV SVGTIASIFR LLPDSSGTIN DVLRCGKEMV AACYAMYGSS 

       190        200        210        220        230        240 
THLVLTLGDG VDGFTLDTNL GEFILTHPNL RIPPQKAIYS INEGNTLYWN ETIRTFIEKV 

       250        260        270        280        290        300 
KQPQADNNNK PFSARYVGSM VADVHRTFLY GGLFAYPCDK KSPNGKLRLL YEAFPMAFLM 

       310        320        330        340 
EQAGGKAVND RGERILDLVP SHIHDKSSIW LGSSGEIDKF LDHIGKSQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the gene for fructose-1,6-bisphosphatase from Saccharomyces cerevisiae and Schizosaccharomyces pombe. Sequence, protein homology, and expression during growth on glucose." Rogers D.T., Hiller E., Mitsock L., Orr E. J. Biol. Chem. 263:6051-6057(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Isolation and primary structure of the gene encoding fructose-1,6-bisphosphatase from Saccharomyces cerevisiae." Entian K.-D., Vogel R.F., Rose M., Hofmann L., Mecke D. FEBS Lett. 236:195-200(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"Amino acid sequence homology among fructose-1,6-bisphosphatases." Marcus F., Gontero B., Harrsch P.B., Rittenhouse J. Biochem. Biophys. Res. Commun. 135:374-381(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16; 83-97; 256-280; 289-306 AND 327-346.
[7]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y00754 Genomic DNA. Translation: CAA68723.1. J03207 Genomic DNA. Translation: AAA34603.1. U19103 Genomic DNA. Translation: AAB67579.1. AY692816 Genomic DNA. Translation: AAT92835.1. BK006945 Genomic DNA. Translation: DAA09679.1.
PIR	PABY. S01127.
RefSeq	NP_013481.3. NM_001182266.3.
3D structure databases
ProteinModelPortal	P09201.
SMR	P09201. Positions 17-342.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3986N.
IntAct	P09201. 6 interactions.
MINT	MINT-562945.
STRING	4932.YLR377C.
Proteomic databases
PaxDb	P09201.
PeptideAtlas	P09201.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR377C; YLR377C; YLR377C.
GeneID	851092.
KEGG	sce:YLR377C. sce:YLR380W.
Organism-specific databases
SGD	S000004369. FBP1.
Phylogenomic databases
eggNOG	COG0158.
GeneTree	ENSGT00390000015513.
HOGENOM	HOG000191265.
KO	K03841.
OMA	CQEEDKA.
OrthoDB	EOG4V9Z0B.
Enzyme and pathway databases
UniPathway	UPA00138.
Gene expression databases
Genevestigator	P09201.
GermOnline	YLR377C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000146. FBPase_class-1/SBPase. IPR020548. Fructose_bisphosphatase_AS. [Graphical view]
PANTHER	PTHR11556. PTHR11556. 1 hit.
Pfam	PF00316. FBPase. 1 hit. [Graphical view]
PIRSF	PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTS	PR00115. F16BPHPHTASE.
PROSITE	PS00124. FBPASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967768.

Entry information

Entry name

F16P_YEAST

Accession

Primary (citable) accession number: P09201
Secondary accession number(s): D6VZ13

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XII

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents