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Q3SZB7 (F16P1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-1,6-bisphosphatase 1

Short name=FBPase 1
EC=3.1.3.11
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase 1
Gene names
Name:FBP1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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. Fructose-2,6-biphosphate acts as competitive inhibitor. Fructose-2,6-biphosphate and AMP have synergistic effects By similarity.

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the FBPase class 1 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Gluconeogenesis
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   PTMAcetylation
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcellular response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to magnesium ion

Inferred from sequence or structural similarity. Source: UniProtKB

fructose 6-phosphate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

gluconeogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of Ras protein signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of glycolysis

Inferred from sequence or structural similarity. Source: UniProtKB

protein homotetramerization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of gluconeogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

soluble fraction

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionAMP binding

Inferred from sequence or structural similarity. Source: UniProtKB

fructose 1,6-bisphosphate 1-phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

monosaccharide binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 338337Fructose-1,6-bisphosphatase 1
PRO_0000247322

Regions

Nucleotide binding18 – 225AMP By similarity
Nucleotide binding28 – 325AMP By similarity
Nucleotide binding113 – 1142AMP By similarity
Region122 – 1254Substrate binding By similarity
Region213 – 2164Substrate binding By similarity
Region244 – 2496Substrate binding By similarity
Region275 – 2773Substrate binding By similarity

Sites

Metal binding691Magnesium 1 By similarity
Metal binding981Magnesium 1 By similarity
Metal binding981Magnesium 2 By similarity
Metal binding1191Magnesium 2 By similarity
Metal binding1191Magnesium 3 By similarity
Metal binding1211Magnesium 2; via carbonyl oxygen By similarity
Metal binding1221Magnesium 3 By similarity
Metal binding2811Magnesium 3 By similarity
Binding site1411AMP
Binding site2651Substrate By similarity

Amino acid modifications

Modified residue21N-acetylthreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3SZB7 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 83EB68040BC2664F

FASTA33836,728
        10         20         30         40         50         60 
MTDQAAFDTN IVTVTRFVME EGRKARGTGE MTQLLNSLCT AVKAISTAVR KAGIAHLYGI 

        70         80         90        100        110        120 
AGTTNVTGDQ VKKLDVLSND LVVNVLKSSF ATCVLVSEED EHAIIVEPEK RGKYVVCFDP 

       130        140        150        160        170        180 
LDGSSNIDCL VSIGTIFGIY KKISKDDPSE KDALQPGRNL VAAGYALYGS ATMLVLAMAN 

       190        200        210        220        230        240 
GVNCFMLDPA IGEFILVDRD VKIKKKGSIY SLNEGYAKDF DPALTEYVQR KKFPPDNSAP 

       250        260        270        280        290        300 
YGARYVGSMV ADVHRTLVYG GIFMYPANKK SPSGKLRLLY ECNPMAYVIE KAGGMATTGK 

       310        320        330 
ETVLDIVPTD IHQKSPIILG SPEDVTEFLE IYKKHAAK 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC102974 mRNA. Translation: AAI02975.1.
IPIIPI00704584.
RefSeqNP_001029619.1. NM_001034447.1.
UniGeneBt.24314.

3D structure databases

ProteinModelPortalQ3SZB7.
SMRQ3SZB7. Positions 7-338.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3SZB7.

Proteomic databases

PRIDEQ3SZB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000012835; ENSBTAP00000012835; ENSBTAG00000009733.
GeneID513483.
KEGGbta:513483.

Organism-specific databases

CTD2203.

Phylogenomic databases

eggNOGmaNOG08767.
GeneTreeENSGT00390000015513.
HOVERGENHBG005627.
InParanoidQ3SZB7.
OrthoDBEOG4P8FJF.
PhylomeDBQ3SZB7.

Family and domain databases

InterProIPR000146. FBPase_class-1/SBPase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
KOK03841.
PANTHERPTHR11556. In_FB_phphtase. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFPIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSPR00115. F16BPHPHTASE.
PROSITEPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF16P1_BOVIN
AccessionPrimary (citable) accession number: Q3SZB7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 57 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families