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Protein

Fructose-1,6-bisphosphatase

Gene

fbp1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi85 – 851Magnesium 1By similarity
Metal bindingi114 – 1141Magnesium 1By similarity
Metal bindingi114 – 1141Magnesium 2By similarity
Metal bindingi133 – 1331Magnesium 2By similarity
Metal bindingi133 – 1331Magnesium 3By similarity
Metal bindingi135 – 1351Magnesium 2; via carbonyl oxygenBy similarity
Metal bindingi136 – 1361Magnesium 3By similarity
Binding sitei227 – 2271SubstrateBy similarity
Binding sitei259 – 2591SubstrateBy similarity
Binding sitei279 – 2791SubstrateBy similarity
Binding sitei288 – 2881SubstrateBy similarity
Metal bindingi294 – 2941Magnesium 3By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi44 – 485AMPBy similarity
Nucleotide bindingi127 – 1282AMPBy similarity

GO - Molecular functioni

  • fructose 1,6-bisphosphate 1-phosphatase activity Source: PomBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cellular response to glucose starvation Source: PomBase
  • dephosphorylation Source: GOC
  • gluconeogenesis Source: PomBase
  • glycerol catabolic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-SPO-70263. 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
ORF Names:SPBC1198.14c, SPBC660.04c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1198.14c.
PomBaseiSPBC1198.14c. fbp1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 347347Fructose-1,6-bisphosphatasePRO_0000200510Add
BLAST

Proteomic databases

MaxQBiP09202.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi276574. 32 interactions.
MINTiMINT-4687092.

Structurei

3D structure databases

ProteinModelPortaliP09202.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni136 – 1394Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the FBPase class 1 family.Curated

Phylogenomic databases

HOGENOMiHOG000191265.
InParanoidiP09202.
KOiK03841.
OMAiEANPMSW.
OrthoDBiEOG77HDQH.
PhylomeDBiP09202.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
InterProiIPR000146. FBPase_class-1.
IPR033391. FBPase_N.
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.

P09202-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKDLDEIDT DIVTLSSFIL QEQRRYNQKH KNEEGKPCII QEASGELSLL
60 70 80 90 100
LNSLQFSFKF IANTIRKAEL VNLIGLSGIV NSTGDEQKKL DKICNDIFIT
110 120 130 140 150
AMKSNGCCKL IVSEEEEDLI VVDSNGSYAV TCDPIDGSSN IDAGVSVGTI
160 170 180 190 200
FGIYKLRPGS QGDISDVLRP GKEMVAAGYT MYGASAHLLL TTGHRVNGFT
210 220 230 240 250
LDTDIGEFIL THRNMKMPLQ HSIYSINEGY TAFWDEKIAR FIAHLKESTP
260 270 280 290 300
DKKPYSARYI GSMVADMHRT ILYGGLFAYP CSKGNNGKLR LLYECFPMAF
310 320 330 340
LVEQAGGIAV NDKGDRILDL VPKTLHGKSS IWLGSKHEVE EYINFIK
Length:347
Mass (Da):38,525
Last modified:July 1, 1989 - v1
Checksum:i54E3371862106FF0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03213 Genomic DNA. Translation: AAA35304.1.
CU329671 Genomic DNA. Translation: CAB91189.1.
PIRiT43294. B28653.
RefSeqiNP_595083.2. NM_001020990.3.

Genome annotation databases

EnsemblFungiiSPBC1198.14c.1; SPBC1198.14c.1:pep; SPBC1198.14c.
GeneIDi2540031.
KEGGispo:SPBC1198.14c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03213 Genomic DNA. Translation: AAA35304.1.
CU329671 Genomic DNA. Translation: CAB91189.1.
PIRiT43294. B28653.
RefSeqiNP_595083.2. NM_001020990.3.

3D structure databases

ProteinModelPortaliP09202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276574. 32 interactions.
MINTiMINT-4687092.

Proteomic databases

MaxQBiP09202.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1198.14c.1; SPBC1198.14c.1:pep; SPBC1198.14c.
GeneIDi2540031.
KEGGispo:SPBC1198.14c.

Organism-specific databases

EuPathDBiFungiDB:SPBC1198.14c.
PomBaseiSPBC1198.14c. fbp1.

Phylogenomic databases

HOGENOMiHOG000191265.
InParanoidiP09202.
KOiK03841.
OMAiEANPMSW.
OrthoDBiEOG77HDQH.
PhylomeDBiP09202.

Enzyme and pathway databases

UniPathwayiUPA00138.
ReactomeiR-SPO-70263. Gluconeogenesis.

Miscellaneous databases

NextBioi20801173.
PROiP09202.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
InterProiIPR000146. FBPase_class-1.
IPR033391. FBPase_N.
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. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiF16P_SCHPO
AccessioniPrimary (citable) accession number: P09202
Secondary accession number(s): Q9P6H8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 11, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.