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P09201 (F16P_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate. HAMAP-Rule MF_01855

Cofactor

Binds 3 magnesium ions per subunit By similarity. HAMAP-Rule MF_01855

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. HAMAP-Rule MF_01855

Pathway

Carbohydrate biosynthesis; gluconeogenesis. HAMAP-Rule MF_01855

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01855

Miscellaneous

Present with 589 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the FBPase class 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 348347Fructose-1,6-bisphosphatase HAMAP-Rule MF_01855
PRO_0000200511

Regions

Nucleotide binding38 – 425AMP By similarity
Nucleotide binding122 – 1232AMP By similarity
Region131 – 1344Substrate binding By similarity

Sites

Metal binding791Magnesium 1 By similarity
Metal binding1081Magnesium 1 By similarity
Metal binding1081Magnesium 2 By similarity
Metal binding1281Magnesium 2 By similarity
Metal binding1281Magnesium 3 By similarity
Metal binding1301Magnesium 2; via carbonyl oxygen By similarity
Metal binding1311Magnesium 3 By similarity
Metal binding2921Magnesium 3 By similarity
Binding site2221Substrate By similarity
Binding site2561Substrate By similarity
Binding site2761Substrate By similarity
Binding site2861Substrate By similarity

Amino acid modifications

Modified residue121Phosphoserine Ref.8

Experimental info

Sequence conflict2781C → D AA sequence Ref.6

Sequences

Sequence LengthMass (Da)Tools
P09201 [UniParc].

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

FASTA34838,263
        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' 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. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., 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].
[8]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [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.
PIRPABY. S01127.
RefSeqNP_013481.3. NM_001182266.3.

3D structure databases

ProteinModelPortalP09201.
SMRP09201. Positions 17-342.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31636. 65 interactions.
DIPDIP-3986N.
IntActP09201. 6 interactions.
MINTMINT-562945.
STRING4932.YLR377C.

Proteomic databases

PaxDbP09201.
PeptideAtlasP09201.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR377C; YLR377C; YLR377C.
GeneID851092.
KEGGsce:YLR377C.

Organism-specific databases

SGDS000004369. FBP1.

Phylogenomic databases

eggNOGCOG0158.
GeneTreeENSGT00390000015513.
HOGENOMHOG000191265.
KOK03841.
OMAAYQIPGK.
OrthoDBEOG77HDQH.

Enzyme and pathway databases

BioCycYEAST:YLR377C-MONOMER.
UniPathwayUPA00138.

Gene expression databases

GenevestigatorP09201.

Family and domain databases

HAMAPMF_01855. FBPase_class1.
InterProIPR000146. FBPase_class-1/SBPase.
IPR028343. FBPtase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERPTHR11556. PTHR11556. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFPIRSF500210. FBPtase. 1 hit.
PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSPR00115. F16BPHPHTASE.
PROSITEPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio967768.
PROP09201.

Entry information

Entry nameF16P_YEAST
AccessionPrimary (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: April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways