Putative 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase YLR345W - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q06137 (YL345_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 84. History...

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

Documents (2) |

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:
Putative 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase YLR345W

Including the following 2 domains:

6-phosphofructo-2-kinase
EC=2.7.1.105
Fructose-2,6-bisphosphatase
EC=3.1.3.46

Gene names

Ordered Locus Names:

YLR345W

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	509 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Synthesis and degradation of fructose 2,6-bisphosphate By similarity.
Catalytic activity	Beta-D-fructose 2,6-bisphosphate + H₂O = D-fructose 6-phosphate + phosphate. ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Ref.3.
Induction	Expression is under the control of the RFX1 transcription factor. Ref.5
Miscellaneous	Present with 3380 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	In the C-terminal section; belongs to the phosphoglycerate mutase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	fructose 2,6-bisphosphate metabolic process Non-traceable author statement Ref.5. Source: SGD regulation of glycolysis Non-traceable author statement Ref.5. Source: SGD
Cellular component	cytoplasm Inferred from direct assay Ref.3. Source: SGD
Molecular function	6-phosphofructo-2-kinase activity Non-traceable author statement Ref.5. Source: SGD ATP binding Inferred from electronic annotation. Source: UniProtKB-KW fructose-2,6-bisphosphate 2-phosphatase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
FBP26	P32604	3	EBI-33827,EBI-6749
MTR3	P48240	3	EBI-33827,EBI-1749
SFH1	Q06168	3	EBI-33827,EBI-35813

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 509

509

Putative 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase YLR345W

PRO_0000268185

Regions

Nucleotide binding

90 – 97

ATP By similarity

Region

6 – 291

286

6-phosphofructo-2-kinase By similarity

Region

292 – 466

175

Fructose-2,6-bisphosphatase By similarity

Sites

Active site

173

Potential

Active site

459

Proton donor By similarity

Binding site

237

Fructose-6-phosphate By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.7

Modified residue

Phosphoserine Ref.7

Modified residue

104

Phosphothreonine Ref.6

Modified residue

432

Phosphoserine Ref.7

Sequences

Sequence

Length

Mass (Da)

Tools

Q06137 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 29718CA8ECA8EB4E
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FASTA

509

58,386

        10         20         30         40         50         60 
MPNVLSDDEE LLNGLGSEIM KPSRQGNHMA RTVKRWVNKE RATTADLKNV NIDGVHGPVN 

        70         80         90        100        110        120 
TESYISPGQL YSTDSGNLFH AGRILVVLVG LPATSKTLLS VAITRYTRWL GVRTKSFHFS 

       130        140        150        160        170        180 
EYKESAKNIP SDYFCVVPTS KEGVAFVEKL RMQMLNDILA FFNDLSGQLA IYDALNIRKI 

       190        200        210        220        230        240 
DRKNLETTFS EIGVKVLFIE SIVSDQEIMN RNIALALESN DYKGLSTDEA IDEYMRRLSV 

       250        260        270        280        290        300 
NEPYYEMMTH DEELSYIKYI NLGKQIIVKD NIHGYLVNKI VFFLMNLRQK KGCVYFARCG 

       310        320        330        340        350        360 
TSDKDNYIHD EELNEEGIHY SQVLKDFVLQ RIKQKRQAKK NSDSLVEVID GSHDEDLKTS 

       370        380        390        400        410        420 
LIVWTGPRKR THDTALFFSK EGIKVQQRSE LRQLNPGSIA DLTDQQIMDK FPSEYKESLK 

       430        440        450        460        470        480 
DPYHFRFPRA ESYHDLAVRM EPLLLEMEHT SKDILIIAHE STLRVLYGYL MACTCVELPN 

       490        500 
LNFTRDKLVE ISFSPFCNTV ELLNIPLTS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[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]	"Identification of new genes regulated by the Crt1 transcription factor, an effector of the DNA damage checkpoint pathway in Saccharomyces cerevisiae." Zaim J., Speina E., Kierzek A.M. J. Biol. Chem. 280:28-37(2005) [PubMed: 15494396] [Abstract] Cited for: INDUCTION.
[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 THR-104, 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-6; SER-75 AND SER-432, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U19028 Genomic DNA. Translation: AAB67253.1. BK006945 Genomic DNA. Translation: DAA09650.1.
PIR	S51348.
RefSeq	NP_013449.1. NM_001182234.1.
3D structure databases
HSSP	HSSP built from PDB template 2AXN based on UniProtKB Q16875.
ProteinModelPortal	Q06137.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1500N.
IntAct	Q06137. 16 interactions.
MINT	MINT-398775.
STRING	Q06137.
Proteomic databases
PeptideAtlas	Q06137.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR345W; YLR345W; YLR345W.
GeneID	851059.
KEGG	sce:YLR345W.
NMPDR	fig\|4932.3.peg.4470.
Organism-specific databases
CYGD	YLR345w.
SGD	S000004337. YLR345W.
Phylogenomic databases
eggNOG	fuNOG04023.
GeneTree	EFGT00050000005287.
HOGENOM	HBG395770.
OrthoDB	EOG4QNR4J.
Gene expression databases
ArrayExpress	Q06137.
Genevestigator	Q06137.
GermOnline	YLR345W. 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. [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]
ProtoNet	Search...
Other
NextBio	967684.

Entry information

Entry name

YL345_YEAST

Accession

Primary (citable) accession number: Q06137
Secondary accession number(s): D6VYY4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 84 of the entry and version 1 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

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

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

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