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Protein

Fructose-2,6-bisphosphatase

Gene

FBP26

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This is predominantly if not solely a fructose-2,6-bisphosphatase.

Catalytic activityi

Beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531Fructose 6-phosphateBy similarity
Binding sitei78 – 781Fructose 6-phosphateBy similarity
Active sitei104 – 1041Sequence analysis
Binding sitei106 – 1061Fructose 6-phosphateBy similarity
Binding sitei112 – 1121Fructose 6-phosphateBy similarity
Binding sitei169 – 1691Fructose 6-phosphateBy similarity
Binding sitei173 – 1731Fructose 6-phosphateBy similarity
Binding sitei231 – 2311Fructose 2,6-bisphosphateBy similarity
Sitei231 – 2311Transition state stabilizerBy similarity
Active sitei232 – 2321Tele-phosphohistidine intermediateBy similarity
Binding sitei238 – 2381Fructose 2,6-bisphosphateBy similarity
Sitei238 – 2381Transition state stabilizerBy similarity
Binding sitei244 – 2441Fructose 2,6-bisphosphate; via amide nitrogenBy similarity
Active sitei302 – 3021Proton donor/acceptorBy similarity
Binding sitei313 – 3131Fructose 2,6-bisphosphateBy similarity
Binding sitei327 – 3271Fructose 2,6-bisphosphateBy similarity
Binding sitei331 – 3311Fructose 2,6-bisphosphateBy similarity
Binding sitei342 – 3421Fructose 2,6-bisphosphateBy similarity
Sitei367 – 3671Transition state stabilizerBy similarity
Binding sitei368 – 3681Fructose 2,6-bisphosphateBy similarity
Binding sitei372 – 3721Fructose 2,6-bisphosphateBy similarity
Binding sitei404 – 4041ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 289ATPBy similarity
Nucleotide bindingi143 – 1486ATPBy similarity
Nucleotide bindingi324 – 3274ATPBy similarity
Nucleotide bindingi368 – 3725ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • fructose-2,6-bisphosphate 2-phosphatase activity Source: SGD

GO - Biological processi

  • fructose 2,6-bisphosphate metabolic process Source: InterPro
  • fructose metabolic process Source: InterPro
  • glucose metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YJL155C-MONOMER.
ReactomeiR-SCE-70171. Glycolysis.
R-SCE-70263. Gluconeogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
Gene namesi
Name:FBP26
Ordered Locus Names:YJL155C
ORF Names:J0575
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL155C.
SGDiS000003691. FBP26.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 452452Fructose-2,6-bisphosphatasePRO_0000179975Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei435 – 4351PhosphoserineCombined sources
Modified residuei446 – 4461PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32604.
PRIDEiP32604.

PTM databases

iPTMnetiP32604.

Expressioni

Inductioni

Inhibited by fructose 6-P, activated by glycerol 3-P.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
YLR345WQ061373EBI-6749,EBI-33827

Protein-protein interaction databases

BioGridi33605. 42 interactions.
DIPiDIP-2593N.
IntActiP32604. 5 interactions.
MINTiMINT-425348.

Structurei

3D structure databases

ProteinModelPortaliP32604.
SMRiP32604. Positions 16-424.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2232236-phosphofructo-2-kinaseBy similarityAdd
BLAST
Regioni224 – 452229Fructose-2,6-bisphosphataseAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the phosphoglycerate mutase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
InParanoidiP32604.
KOiK19029.
OMAiFIQRIEC.
OrthoDBiEOG7P8PJ6.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR027417. P-loop_NTPase.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view]
PANTHERiPTHR10606. PTHR10606. 1 hit.
PfamiPF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view]
PRINTSiPR00991. 6PFRUCTKNASE.
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32604-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGYSTISNDN DIKVCVIMVG LPARGKSFIS QKIIRYLSWL SIKAKCFNVG
60 70 80 90 100
NYRRDVSGNV PMDAEFFNFE NTDNFKLREL AAQNAIKDIV NFFTKEDGSV
110 120 130 140 150
AVFDATNSTR KRRKWLKDIC EKNNIQPMFL ESWSNDHELI INNAKDIGST
160 170 180 190 200
SPDYENSEPH VAEADFLERI RQYERFYEPL DPQKDKDMTF IKLVNIIEEV
210 220 230 240 250
VINKIRTYLE SRIVFYVMNI RPKPKYIWLS RHGESIYNVE KKIGGDSSLS
260 270 280 290 300
ERGFQYAKKL EQLVKESAGE INLTVWTSTL KRTQQTANYL PYKKLQWKAL
310 320 330 340 350
DELDAGVCDG MTYEEIEKEY PEDFKARDND KYEYRYRGGE SYRDVVIRLE
360 370 380 390 400
PVIMELERQE NVLIITHQAV LRCIYAYFMN VPQEESPWMS IPLHTLIKLE
410 420 430 440 450
PRAYGTKVTK IKANIPAVST YKEKGTSQVG ELSQSSTKLH QLLNDSPLED

KF
Length:452
Mass (Da):52,595
Last modified:November 1, 1995 - v2
Checksum:i228766A302F32F82
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti199 – 1991E → Q in AAB22823 (PubMed:1322693).Curated
Sequence conflicti362 – 3621V → E in AAB22823 (PubMed:1322693).Curated
Sequence conflicti448 – 4492LE → FQ in AAB22823 (PubMed:1322693).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S42124 Genomic DNA. Translation: AAB22823.1.
Z49430 Genomic DNA. Translation: CAA89450.1.
BK006943 Genomic DNA. Translation: DAA08648.1.
PIRiS56938.
RefSeqiNP_012380.1. NM_001181588.1.

Genome annotation databases

EnsemblFungiiYJL155C; YJL155C; YJL155C.
GeneIDi853286.
KEGGisce:YJL155C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S42124 Genomic DNA. Translation: AAB22823.1.
Z49430 Genomic DNA. Translation: CAA89450.1.
BK006943 Genomic DNA. Translation: DAA08648.1.
PIRiS56938.
RefSeqiNP_012380.1. NM_001181588.1.

3D structure databases

ProteinModelPortaliP32604.
SMRiP32604. Positions 16-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33605. 42 interactions.
DIPiDIP-2593N.
IntActiP32604. 5 interactions.
MINTiMINT-425348.

PTM databases

iPTMnetiP32604.

Proteomic databases

MaxQBiP32604.
PRIDEiP32604.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL155C; YJL155C; YJL155C.
GeneIDi853286.
KEGGisce:YJL155C.

Organism-specific databases

EuPathDBiFungiDB:YJL155C.
SGDiS000003691. FBP26.

Phylogenomic databases

GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
InParanoidiP32604.
KOiK19029.
OMAiFIQRIEC.
OrthoDBiEOG7P8PJ6.

Enzyme and pathway databases

BioCyciYEAST:YJL155C-MONOMER.
ReactomeiR-SCE-70171. Glycolysis.
R-SCE-70263. Gluconeogenesis.

Miscellaneous databases

PROiP32604.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR027417. P-loop_NTPase.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view]
PANTHERiPTHR10606. PTHR10606. 1 hit.
PfamiPF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view]
PRINTSiPR00991. 6PFRUCTKNASE.
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The yeast FBP26 gene codes for a fructose-2,6-bisphosphatase."
    Paravicini G., Kretschmer M.
    Biochemistry 31:7126-7133(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  6. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435 AND SER-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiF26_YEAST
AccessioniPrimary (citable) accession number: P32604
Secondary accession number(s): D6VW32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: November 1, 1995
Last modified: July 6, 2016
This is version 157 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 1680 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

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.