Fructose-1,6-bisphosphatase - Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast)

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Q05079 (F16P_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 80. History...

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

Documents (2) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Fructose-1,6-bisphosphatase
Short name=FBPase
EC=3.1.3.11

Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase

Gene names

Name:	FBP1
Ordered Locus Names:	KLLA0E01210g

Organism

Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

284590 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	D-fructose 1,6-bisphosphate + H₂O = D-fructose 6-phosphate + phosphate.
Cofactor	Binds 3 magnesium ions per subunit By similarity.
Enzyme regulation	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.
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the FBPase class 1 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	fructose 1,6-bisphosphate 1-phosphatase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Probable

Chain

2 – 355

354

Fructose-1,6-bisphosphatase

PRO_0000200509

Regions

Nucleotide binding

37 – 41

AMP By similarity

Nucleotide binding

121 – 122

AMP By similarity

Region

130 – 133

Substrate binding By similarity

Sites

Metal binding

Magnesium 1 By similarity

Metal binding

107

Magnesium 1 By similarity

Metal binding

107

Magnesium 2 By similarity

Metal binding

127

Magnesium 2 By similarity

Metal binding

127

Magnesium 3 By similarity

Metal binding

129

Magnesium 2; via carbonyl oxygen By similarity

Metal binding

130

Magnesium 3 By similarity

Metal binding

300

Magnesium 3 By similarity

Binding site

230

Substrate By similarity

Binding site

264

Substrate By similarity

Binding site

284

Substrate By similarity

Binding site

294

Substrate By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q05079 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 3E24B69D32980AF6
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FASTA

355

38,899

        10         20         30         40         50         60 
MAGIKHRRDS AESINTDIIT LSRFILDQQH LSAKNATGEF SMLLNSLQFA FKFISQTIRR 

        70         80         90        100        110        120 
AELVNLIGLA GASNSTGDQQ KKLDVLGDEI FINAMKASGN VKVLVSEEQE DLIVFRNSPG 

       130        140        150        160        170        180 
KYAVCCDPID GSSNLDAGVS VGTIVSLFKI HENQNGNSGE EDSEGTINDV ARCGREMVAA 

       190        200        210        220        230        240 
CYTMYGASTH LVLTTGAGVN GFTLDNNLGE FILTYPELRL PEQKSIYSIN EGNTCYWEPT 

       250        260        270        280        290        300 
IADFIAKLKE NSEENNGKPY SARYIGSMVA DVHRTLLYGG LFSYPGDKKN PNGKLRLLYE 

       310        320        330        340        350 
AFPMAFLVEQ AGGKAVNDRG ERILDLVPQH IHDKSSIWLG SSGDVDKYLK HIGKL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Fructose-1,6-bisphosphatase of the yeast Kluyveromyces lactis." Zaror I., Marcus F., Moyer D.L., Tung J., Shuster J.R. Eur. J. Biochem. 212:193-199(1993) [PubMed: 8383039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SD11.
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X70181 Genomic DNA. Translation: CAA49728.1. CR382125 Genomic DNA. Translation: CAG99090.1.
PIR	S29397.
RefSeq	XP_454003.1. XM_454003.1.
3D structure databases
ProteinModelPortal	Q05079.
ModBase	Search...
Protein-protein interaction databases
STRING	Q05079.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2894286.
GenomeReviews	Gene locus KLLA0E01210g in contig CR382125_GR.
KEGG	kla:KLLA0E01211g.
Phylogenomic databases
eggNOG	fuNOG04311.
HOGENOM	HBG731261.
OMA	YGSATMV.
OrthoDB	EOG4V9Z0B.
Family and domain databases
InterPro	IPR000146. FBPase_class-1/SBPase. IPR020548. Fructose_bisphosphatase_AS. [Graphical view]
KO	K03841.
PANTHER	PTHR11556. In_FB_phphtase. 1 hit.
Pfam	PF00316. FBPase. 1 hit. [Graphical view]
PIRSF	PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTS	PR00115. F16BPHPHTASE.
PROSITE	PS00124. FBPASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

F16P_KLULA

Accession

Primary (citable) accession number: Q05079

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 80 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents