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Protein

Fructose-1,6-bisphosphatase

Gene

FBP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 3 Mg2+ ions per subunit.By similarity

Enzyme regulationi

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).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi79 – 791Magnesium 1By similarity
Metal bindingi108 – 1081Magnesium 1By similarity
Metal bindingi108 – 1081Magnesium 2By similarity
Metal bindingi128 – 1281Magnesium 2By similarity
Metal bindingi128 – 1281Magnesium 3By similarity
Metal bindingi130 – 1301Magnesium 2; via carbonyl oxygenBy similarity
Metal bindingi131 – 1311Magnesium 3By similarity
Binding sitei222 – 2221SubstrateBy similarity
Binding sitei256 – 2561SubstrateBy similarity
Binding sitei276 – 2761SubstrateBy similarity
Binding sitei286 – 2861SubstrateBy similarity
Metal bindingi292 – 2921Magnesium 3By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi38 – 425AMPBy similarity
Nucleotide bindingi122 – 1232AMPBy similarity

GO - Molecular functioni

  1. fructose 1,6-bisphosphate 1-phosphatase activity Source: SGD
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. dephosphorylation Source: GOC
  2. gluconeogenesis Source: SGD
  3. reactive oxygen species metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YLR377C-MONOMER.
BRENDAi3.1.3.11. 984.
ReactomeiREACT_286539. Gluconeogenesis.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-1,6-bisphosphatase (EC:3.1.3.11)
Short name:
FBPase
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase
Gene namesi
Name:FBP1
Ordered Locus Names:YLR377C
ORF Names:L8039.18
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR377C.
SGDiS000004369. FBP1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: SGD
  2. periplasmic space Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 348347Fructose-1,6-bisphosphatasePRO_0000200511Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP09201.
PeptideAtlasiP09201.

Expressioni

Gene expression databases

GenevestigatoriP09201.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi31636. 65 interactions.
DIPiDIP-3986N.
IntActiP09201. 6 interactions.
MINTiMINT-562945.
STRINGi4932.YLR377C.

Structurei

3D structure databases

ProteinModelPortaliP09201.
SMRiP09201. Positions 17-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni131 – 1344Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the FBPase class 1 family.Curated

Phylogenomic databases

eggNOGiCOG0158.
GeneTreeiENSGT00390000015513.
HOGENOMiHOG000191265.
InParanoidiP09201.
KOiK03841.
OMAiNGVNCFM.
OrthoDBiEOG77HDQH.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
InterProiIPR000146. FBPase_class-1/SBPase.
IPR028343. FBPtase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERiPTHR11556. PTHR11556. 1 hit.
PfamiPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFiPIRSF500210. FBPtase. 1 hit.
PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSiPR00115. F16BPHPHTASE.
PROSITEiPS00124. FBPASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09201-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTLVNGPRR DSTEGFDTDI ITLPRFIIEH QKQFKNATGD FTLVLNALQF
60 70 80 90 100
AFKFVSHTIR RAELVNLVGL AGASNFTGDQ QKKLDVLGDE IFINAMRASG
110 120 130 140 150
IIKVLVSEEQ EDLIVFPTNT GSYAVCCDPI DGSSNLDAGV SVGTIASIFR
160 170 180 190 200
LLPDSSGTIN DVLRCGKEMV AACYAMYGSS THLVLTLGDG VDGFTLDTNL
210 220 230 240 250
GEFILTHPNL RIPPQKAIYS INEGNTLYWN ETIRTFIEKV KQPQADNNNK
260 270 280 290 300
PFSARYVGSM VADVHRTFLY GGLFAYPCDK KSPNGKLRLL YEAFPMAFLM
310 320 330 340
EQAGGKAVND RGERILDLVP SHIHDKSSIW LGSSGEIDKF LDHIGKSQ
Length:348
Mass (Da):38,263
Last modified:January 23, 2007 - v2
Checksum:iBCFC0984A086094B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti278 – 2781C → D AA sequence (PubMed:3008716).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS01127. PABY.
RefSeqiNP_013481.3. NM_001182266.3.

Genome annotation databases

EnsemblFungiiYLR377C; YLR377C; YLR377C.
GeneIDi851092.
KEGGisce:YLR377C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS01127. PABY.
RefSeqiNP_013481.3. NM_001182266.3.

3D structure databases

ProteinModelPortaliP09201.
SMRiP09201. Positions 17-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31636. 65 interactions.
DIPiDIP-3986N.
IntActiP09201. 6 interactions.
MINTiMINT-562945.
STRINGi4932.YLR377C.

Proteomic databases

PaxDbiP09201.
PeptideAtlasiP09201.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR377C; YLR377C; YLR377C.
GeneIDi851092.
KEGGisce:YLR377C.

Organism-specific databases

EuPathDBiFungiDB:YLR377C.
SGDiS000004369. FBP1.

Phylogenomic databases

eggNOGiCOG0158.
GeneTreeiENSGT00390000015513.
HOGENOMiHOG000191265.
InParanoidiP09201.
KOiK03841.
OMAiNGVNCFM.
OrthoDBiEOG77HDQH.

Enzyme and pathway databases

UniPathwayiUPA00138.
BioCyciYEAST:YLR377C-MONOMER.
BRENDAi3.1.3.11. 984.
ReactomeiREACT_286539. Gluconeogenesis.

Miscellaneous databases

NextBioi967768.
PROiP09201.

Gene expression databases

GenevestigatoriP09201.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
InterProiIPR000146. FBPase_class-1/SBPase.
IPR028343. FBPtase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERiPTHR11556. PTHR11556. 1 hit.
PfamiPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFiPIRSF500210. FBPtase. 1 hit.
PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSiPR00115. F16BPHPHTASE.
PROSITEiPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. 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. 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].

Entry informationi

Entry nameiF16P_YEAST
AccessioniPrimary (citable) accession number: P09201
Secondary accession number(s): D6VZ13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 589 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.