Fructose-2,6-bisphosphatase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32604 (F26_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Fructose-2,6-bisphosphatase
EC=3.1.3.46

Gene names

Name:	FBP26
Ordered Locus Names:	YJL155C
ORF Names:	J0575

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This is predominantly if not solely a fructose-2,6-bisphosphatase.
Catalytic activity	Beta-D-fructose 2,6-bisphosphate + H₂O = D-fructose 6-phosphate + phosphate.
Induction	Inhibited by fructose 6-P, activated by glycerol 3-P.
Miscellaneous	Present with 1680 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	In the C-terminal section; belongs to the phosphoglycerate mutase family.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	fructose 2,6-bisphosphate metabolic process Inferred from electronic annotation. Source: InterPro glucose metabolic process Inferred from mutant phenotype Ref.1. Source: SGD
Molecular function	6-phosphofructo-2-kinase activity Inferred from electronic annotation. Source: InterPro ATP binding Inferred from electronic annotation. Source: UniProtKB-KW fructose-2,6-bisphosphate 2-phosphatase activity Inferred from mutant phenotype Ref.1. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
YLR345W	Q06137	3	EBI-6749,EBI-33827

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 452

452

Fructose-2,6-bisphosphatase

PRO_0000179975

Regions

Nucleotide binding

20 – 27

ATP By similarity

Region

1 – 223

223

6-phosphofructo-2-kinase By similarity

Region

224 – 452

229

Fructose-2,6-bisphosphatase

Sites

Active site

104

Potential

Active site

232

Tele-phosphohistidine intermediate By similarity

Active site

302

Potential

Active site

367

Proton donor By similarity

Binding site

Fructose-6-phosphate By similarity

Binding site

169

Fructose-6-phosphate By similarity

Amino acid modifications

Modified residue

151

Phosphoserine Ref.6 Ref.7

Modified residue

433

Phosphoserine Ref.7

Modified residue

435

Phosphoserine Ref.7

Modified residue

436

Phosphoserine Ref.7

Modified residue

446

Phosphoserine Ref.5 Ref.6 Ref.7

Experimental info

Sequence conflict

199

E → Q in AAB22823. Ref.1

Sequence conflict

362

V → E in AAB22823. Ref.1

Sequence conflict

448 – 449

LE → FQ in AAB22823. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P32604 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 228766A302F32F82
Show »

FASTA

452

52,595

        10         20         30         40         50         60 
MGYSTISNDN DIKVCVIMVG LPARGKSFIS QKIIRYLSWL SIKAKCFNVG NYRRDVSGNV 

        70         80         90        100        110        120 
PMDAEFFNFE NTDNFKLREL AAQNAIKDIV NFFTKEDGSV AVFDATNSTR KRRKWLKDIC 

       130        140        150        160        170        180 
EKNNIQPMFL ESWSNDHELI INNAKDIGST SPDYENSEPH VAEADFLERI RQYERFYEPL 

       190        200        210        220        230        240 
DPQKDKDMTF IKLVNIIEEV VINKIRTYLE SRIVFYVMNI RPKPKYIWLS RHGESIYNVE 

       250        260        270        280        290        300 
KKIGGDSSLS ERGFQYAKKL EQLVKESAGE INLTVWTSTL KRTQQTANYL PYKKLQWKAL 

       310        320        330        340        350        360 
DELDAGVCDG MTYEEIEKEY PEDFKARDND KYEYRYRGGE SYRDVVIRLE PVIMELERQE 

       370        380        390        400        410        420 
NVLIITHQAV LRCIYAYFMN VPQEESPWMS IPLHTLIKLE PRAYGTKVTK IKANIPAVST 

       430        440        450 
YKEKGTSQVG ELSQSSTKLH QLLNDSPLED KF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The yeast FBP26 gene codes for a fructose-2,6-bisphosphatase." Paravicini G., Kretschmer M. Biochemistry 31:7126-7133(1992) [PubMed: 1322693] [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. Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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: 14562106] [Abstract] 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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446, MASS SPECTROMETRY. Strain: ADR376.
[6]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151 AND SER-446, MASS SPECTROMETRY.
[7]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-433; SER-435; SER-436 AND SER-446, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S42124 Genomic DNA. Translation: AAB22823.1. Z49430 Genomic DNA. Translation: CAA89450.1. BK006943 Genomic DNA. Translation: DAA08648.1.
PIR	S56938.
RefSeq	NP_012380.1. NM_001181588.1.
3D structure databases
ProteinModelPortal	P32604.
SMR	P32604. Positions 13-428.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2593N.
IntAct	P32604. 4 interactions.
MINT	MINT-425348.
STRING	P32604.
Proteomic databases
PeptideAtlas	P32604.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YJL155C; YJL155C; YJL155C.
GeneID	853286.
KEGG	sce:YJL155C.
NMPDR	fig\|4932.3.peg.3345.
Organism-specific databases
CYGD	YJL155c.
SGD	S000003691. FBP26.
Phylogenomic databases
eggNOG	fuNOG04567.
GeneTree	EFGT00050000005287.
HOGENOM	HBG395770.
OMA	KEQGQVA.
OrthoDB	EOG44QX8F.
Gene expression databases
ArrayExpress	P32604.
Genevestigator	P32604.
GermOnline	YJL155C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003094. 6Pfruct_kin. IPR013079. 6Phosfructo_kin. IPR016260. Bifunct_6PFK/fruc_bisP_Ptase. IPR013078. His_Pase_superF_clade-1. IPR001345. PG/BPGM_mutase_AS. [Graphical view]
KO	K01103.
PANTHER	PTHR10606. 6Pfruct_kin. 1 hit.
Pfam	PF01591. 6PF2K. 1 hit. PF00300. His_Phos_1. 1 hit. [Graphical view]
PIRSF	PIRSF000709. 6PFK_2-Ptase. 1 hit.
PRINTS	PR00991. 6PFRUCTKNASE.
SMART	SM00855. PGAM. 1 hit. [Graphical view]
PROSITE	PS00175. PG_MUTASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	973585.

Entry information

Entry name

F26_YEAST

Accession

Primary (citable) accession number: P32604
Secondary accession number(s): D6VW32

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	November 1, 1995
Last modified:	December 14, 2011
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome X

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents