Reviewed, UniProtKB/Swiss-Prot P32604 (F26_YEAST)

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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.3
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
Gene Ontology (GO)
Biological process	fructose 2,6-bisphosphate metabolic process Inferred from electronic annotation. Source: InterPro glucose metabolic process Ref.1 Inferred from mutant phenotype. 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 Ref.1 Inferred from mutant phenotype. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARO8	P53090	1	EBI-6749,EBI-2042933
RNR2	P09938	1	EBI-6749,EBI-15240

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	8	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	1	Potential
	Active site	232	1	Tele-phosphohistidine intermediate By similarity
	Active site	302	1	Potential
	Active site	367	1	Proton donor By similarity
	Binding site	78	1	Fructose-6-phosphate By similarity
	Binding site	169	1	Fructose-6-phosphate By similarity
Amino acid modifications
	Modified residue	151	1	Phosphoserine Ref.5 Ref.6
	Modified residue	433	1	Phosphoserine Ref.6
	Modified residue	435	1	Phosphoserine Ref.6
	Modified residue	436	1	Phosphoserine Ref.6
	Modified residue	446	1	Phosphoserine Ref.5 Ref.6 Ref.4
Experimental info
	Sequence conflict	199	1	E → Q in AAB22823. Ref.1
	Sequence conflict	362	1	V → E in AAB22823. Ref.1
	Sequence conflict	448 – 449	2	LE → FQ in AAB22823. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P32604-1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 228766A302F32F82	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

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. , 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: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"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].
[4]	"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.
[5]	"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.
[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: 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
EMBLGenBankDDBJ	S42124 Genomic DNA. Translation: AAB22823.1. Z49430 Genomic DNA. Translation: CAA89450.1.
PIR	S56938.
RefSeq	NP_012380.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2593N.
IntAct	P32604. 9 interactions.
STRING	P32604.
Proteomic databases
PeptideAtlas	P32604.
Genome annotation databases
Ensembl	YJL155C; YJL155C; YJL155C; Saccharomyces cerevisiae. [Genome view]
GeneID	853286.
KEGG	sce:YJL155C.
NMPDR	fig|4932.3.peg.3345.
Organism-specific databases
CYGD	YJL155c.
SGD	S000003691. FBP26.
Phylogenomic databases
HOGENOM	P32604.
OMA	PRLYSAG
OrthoDB	EOG9F4TT5
Enzyme and pathway databases
BRENDA	3.1.3.46. 250.
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. IPR001345. PG/BPGM_mutase_AS. IPR013078. PG_mutase. [Graphical view]
PANTHER	PTHR10606. 6Pfruct_kin. 1 hit.
Pfam	PF01591. 6PF2K. 1 hit. PF00300. PGAM. 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 Resources
NextBio	973585.

Entry information

Entry name

F26_YEAST

Accession

Primary (citable) accession number: P32604

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	November 1, 1995
Last modified:	November 24, 2009
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)