Fructose-1,6-bisphosphatase - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P09201 (F16P_YEAST)

Last modified January 19, 2010. Version 92. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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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.

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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. Ref.6
Sequence similarities	Belongs to the FBPase class 1 family.

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Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from mutant phenotype. Source: SGD oxygen and reactive oxygen species metabolic process Inferred from mutant phenotype. Source: SGD
Cellular component	cytosol Inferred from direct assay. Source: SGD
Molecular function	fructose 1,6-bisphosphate 1-phosphatase activity Ref.2 Inferred from mutant phenotype. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
itself		1	EBI-6744,EBI-6744
KAP95	Q06142	1	EBI-6744,EBI-9145
SRP1	Q02821	1	EBI-6744,EBI-1797
TEM1	P38987	1	EBI-6744,EBI-19113

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.5

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.5

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Sequences

Sequence

Length

Mass (Da)

Tools

P09201-1 [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

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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: 2834361] [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: 2841162] [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: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"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: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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: 3008716] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16; 83-97; 256-280; 289-306 AND 327-346.
[6]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

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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.
PIR	PABY. S01127.
RefSeq	NP_013481.1.
3D structure databases
SMR	P09201. Positions 19-346.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3986N.
IntAct	P09201. 9 interactions.
STRING	P09201.
Proteomic databases
PeptideAtlas	P09201.
Genome annotation databases
Ensembl	YLR377C; YLR377C; YLR377C; Saccharomyces cerevisiae. [Genome view]
GeneID	851092.
KEGG	sce:YLR377C.
NMPDR	fig\|4932.3.peg.4506.
Organism-specific databases
CYGD	YLR377c.
SGD	S000004369. FBP1.
Phylogenomic databases
eggNOG	fuNOG04311.
HOGENOM	HBG731261.
OMA	TCLLVSE.
OrthoDB	EOG92V9ZX.
PhylomeDB	P09201.
Enzyme and pathway databases
BRENDA	3.1.3.11. 250.
Gene expression databases
ArrayExpress	P09201.
Genevestigator	P09201.
GermOnline	YLR377C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000146. Fructose_bisphosphatase. IPR020548. Fructose_bisphosphatase_AS. [Graphical view]
PANTHER	PTHR11556. In_FB_phphtase. 1 hit.
Pfam	PF00316. FBPase. 1 hit. [Graphical view]
PRINTS	PR00115. F16BPHPHTASE.
PROSITE	PS00124. FBPASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	967768.

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Entry information

Entry name

F16P_YEAST

Accession

Primary (citable) accession number: P09201

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents