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P09201

- F16P_YEAST

UniProt

P09201 - F16P_YEAST

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Protein

Fructose-1,6-bisphosphatase

Gene
FBP1, YLR377C, L8039.18
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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.UniRule annotation

Cofactori

Binds 3 magnesium ions per subunit By similarity.UniRule annotation

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.UniRule annotation

Pathwayi

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi38 – 425AMP By similarity
Nucleotide bindingi122 – 1232AMP By 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.
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: Chromosome XII

Organism-specific databases

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-bisphosphataseUniRule annotationPRO_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.UniRule annotation

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.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the FBPase class 1 family.

Phylogenomic databases

eggNOGiCOG0158.
GeneTreeiENSGT00390000015513.
HOGENOMiHOG000191265.
KOiK03841.
OMAiSSFTTCV.
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

MPTLVNGPRR DSTEGFDTDI ITLPRFIIEH QKQFKNATGD FTLVLNALQF    50
AFKFVSHTIR RAELVNLVGL AGASNFTGDQ QKKLDVLGDE IFINAMRASG 100
IIKVLVSEEQ EDLIVFPTNT GSYAVCCDPI DGSSNLDAGV SVGTIASIFR 150
LLPDSSGTIN DVLRCGKEMV AACYAMYGSS THLVLTLGDG VDGFTLDTNL 200
GEFILTHPNL RIPPQKAIYS INEGNTLYWN ETIRTFIEKV KQPQADNNNK 250
PFSARYVGSM VADVHRTFLY GGLFAYPCDK KSPNGKLRLL YEAFPMAFLM 300
EQAGGKAVND RGERILDLVP SHIHDKSSIW LGSSGEIDKF LDHIGKSQ 348
Length:348
Mass (Da):38,263
Last modified:January 23, 2007 - v2
Checksum:iBCFC0984A086094B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti278 – 2781C → D AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S01127. PABY.
RefSeqi NP_013481.3. NM_001182266.3.

3D structure databases

ProteinModelPortali P09201.
SMRi P09201. Positions 17-342.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31636. 65 interactions.
DIPi DIP-3986N.
IntActi P09201. 6 interactions.
MINTi MINT-562945.
STRINGi 4932.YLR377C.

Proteomic databases

PaxDbi P09201.
PeptideAtlasi P09201.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLR377C ; YLR377C ; YLR377C .
GeneIDi 851092.
KEGGi sce:YLR377C.

Organism-specific databases

SGDi S000004369. FBP1.

Phylogenomic databases

eggNOGi COG0158.
GeneTreei ENSGT00390000015513.
HOGENOMi HOG000191265.
KOi K03841.
OMAi SSFTTCV.
OrthoDBi EOG77HDQH.

Enzyme and pathway databases

UniPathwayi UPA00138 .
BioCyci YEAST:YLR377C-MONOMER.

Miscellaneous databases

NextBioi 967768.
PROi P09201.

Gene expression databases

Genevestigatori P09201.

Family and domain databases

HAMAPi MF_01855. FBPase_class1.
InterProi IPR000146. FBPase_class-1/SBPase.
IPR028343. FBPtase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view ]
PANTHERi PTHR11556. PTHR11556. 1 hit.
Pfami PF00316. FBPase. 1 hit.
[Graphical view ]
PIRSFi PIRSF500210. FBPtase. 1 hit.
PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSi PR00115. F16BPHPHTASE.
PROSITEi PS00124. FBPASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: May 14, 2014
This is version 133 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.

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

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