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Reviewed, UniProtKB/Swiss-Prot P00637 (F16P1_RABIT)

Last modified February 9, 2010. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
Synonyms: FBP
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.2
Chain2 – 338337Fructose-1,6-bisphosphatase 1
PRO_0000200501

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
Metal binding1191Magnesium 2
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 By similarity
Binding site2651Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine

Experimental info

Sequence conflict841N → D AA sequence Ref.5
Sequence conflict891S → A AA sequence Ref.5
Sequence conflict931C → S AA sequence Ref.5
Sequence conflict116 – 1172VC → SN AA sequence Ref.5
Sequence conflict122 – 1232DG → VP AA sequence Ref.5
Sequence conflict2681N → D AA sequence Ref.6
Sequence conflict2811E → Q AA sequence Ref.6
Sequence conflict2841Missing AA sequence Ref.6
Sequence conflict3011E → Q AA sequence Ref.6
Sequence conflict308 – 3136PTDIHQ → QTPDH AA sequence Ref.6
Sequence conflict3271E → Q AA sequence Ref.6
Sequence conflict330 – 3312Missing AA sequence Ref.6

Secondary structure

................................................... 338
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00637-1 [UniParc].

Last modified November 24, 2009. Version 4.
Checksum: 2676BF5964461250

FASTA33836,578
        10         20         30         40         50         60 
MADKAPFDTD ISTMTRFVME EGRKAGGTGE MTQLLNSLCT AVKAISTAVR KAGIAHLYGI 

        70         80         90        100        110        120 
AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED KNAIIVEPEK RGKYVVCFDP 

       130        140        150        160        170        180 
LDGSSNIDCL VSIGTIFGIY RKKSTDEPST KDALQPGRNL VAAGYALYGS ATMLVLAGGS 

       190        200        210        220        230        240 
GVNSFMLDPA IGEFILVDKN VKIKKKGNIY SLNEGYAKDF DPAVTEYIQK KKFPPDNSSP 

       250        260        270        280        290        300 
YGARYVGSMV ADVHRTLVYG GIFLYPANKK SPDGKLRLLY ECNPMAFIME KAGGMATTGK 

       310        320        330 
EAILDIVPTD IHQRAPVILG SPDDVQEFLE IYKKHAVK 

« Hide

References

[1]"Fructose-1,6-bisphosphatase. Primary structure of the rabbit liver enzyme. 'Intermediate' variability of an oligomeric protein."
Kaiser R., Olsson H., Erman M., Weeks C.M., Hjelmqvist L., Ghosh D., Joernvall H.
FEBS Lett. 389:249-252(1996) [PubMed: 8766709] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-338.
Tissue: Liver.
[2]"Rabbit liver fructose 1,6-bisphosphatase: the sequence of the amino-terminal region."
El-Dorry H.A., Chu D.K., Dzugaj A., Tsolas O., Pontremoli S., Horecker B.L.
Arch. Biochem. Biophys. 178:200-207(1977) [PubMed: 189691] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-19.
Strain: New Zealand white.
Tissue: Liver.
[3]"Primary structure of the S-peptide formed by digestion of rabbit liver fructose 1,6-biphosphatase with subtilisin."
El-Dorry H.A., Chu D.K., Dzugaj A., Botelho L.H., Pontremoli S., Horecker B.L.
Arch. Biochem. Biophys. 182:763-773(1977) [PubMed: 197893] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-61.
Strain: New Zealand white.
Tissue: Liver.
[4]"Digestion of rabbit liver fructose 1,6-bisphosphatase with subtilisin: sites of cleavage and activity of the modified enzyme."
Botelho L.H., El-Dorry H.A., Crivellaro O., Chu D.K., Pontremoli S., Horecker B.L.
Arch. Biochem. Biophys. 184:535-545(1977) [PubMed: 202200] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-78.
Strain: New Zealand white.
Tissue: Liver.
[5]"Location of lysyl residues at the allosteric site of fructose 1,6-bisphosphatase."
Suda H., Xu G.-J., Kutny R.M., Natalini P., Pontremoli S., Horecker B.L.
Arch. Biochem. Biophys. 217:10-14(1982) [PubMed: 6289748] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 84-123 AND 136-155, ALLOSTERIC REGULATION.
Tissue: Liver.
[6]"Rabbit liver fructose-1,6-bisphosphatase: location of an active site lysyl residue in the COOH-terminal fragment generated by a lysosomal proteinase."
Xu G.J., Natalini P., Suda H., Tsolas O., Dzugaj A., Sun S.C., Pontremoli S., Horecker B.L.
Arch. Biochem. Biophys. 214:688-694(1982) [PubMed: 6284034] [Abstract]
Cited for: PROTEIN SEQUENCE OF 249-289 AND 296-338, ACTIVE SITE.
Tissue: Liver.
[7]"Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 A resolution."
Weeks C.M., Roszak A.W., Erman M., Kaiser R., Joernvall H., Ghosh D.
Acta Crystallogr. D 55:93-102(1999) [PubMed: 10089399] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.

Cross-references

Sequence databases

PIRS70469.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BK4X-ray2.30A2-338[»]
ModBaseSearch...

Phylogenomic databases

eggNOGmaNOG08767.
HOVERGENP00637.

Enzyme and pathway databases

BRENDA3.1.3.11. 255.

Family and domain databases

InterProIPR000146. Fructose_bisphosphatase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERPTHR11556. In_FB_phphtase. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PRINTSPR00115. F16BPHPHTASE.
PROSITEPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF16P1_RABIT
AccessionPrimary (citable) accession number: P00637
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 24, 2009
Last modified: February 9, 2010
This is version 82 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents