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Protein

Fructose-1,6-bisphosphatase 1

Gene

FBP1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain (By similarity).By similarity

Catalytic activityi

D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.

Cofactori

Mg2+By similarityNote: Binds 3 Mg2+ ions per subunit.By similarity

Enzyme regulationi

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

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi69 – 691Magnesium 1By similarity
Metal bindingi98 – 981Magnesium 1By similarity
Metal bindingi98 – 981Magnesium 2
Metal bindingi119 – 1191Magnesium 2
Metal bindingi119 – 1191Magnesium 3By similarity
Metal bindingi121 – 1211Magnesium 2; via carbonyl oxygenBy similarity
Metal bindingi122 – 1221Magnesium 3By similarity
Binding sitei141 – 1411AMPBy similarity
Binding sitei265 – 2651SubstrateBy similarity
Metal bindingi281 – 2811Magnesium 3By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 225AMPBy similarity
Nucleotide bindingi28 – 325AMPBy similarity
Nucleotide bindingi113 – 1142AMPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Gluconeogenesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

SABIO-RKP00637.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-1,6-bisphosphatase 1 (EC:3.1.3.11)
Short name:
FBPase 1
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase 1
Liver FBPase
Gene namesi
Name:FBP1
Synonyms:FBP
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 338337Fructose-1,6-bisphosphatase 1PRO_0000200501Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei151 – 1511N6-succinyllysineBy similarity
Modified residuei216 – 2161PhosphotyrosineBy similarity
Modified residuei245 – 2451PhosphotyrosineBy similarity
Modified residuei265 – 2651PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP00637.

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

Secondary structure

1
338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2512Combined sources
Helixi30 – 4920Combined sources
Turni50 – 534Combined sources
Helixi74 – 8815Combined sources
Beta strandi92 – 976Combined sources
Helixi108 – 1103Combined sources
Beta strandi111 – 12212Combined sources
Helixi126 – 1294Combined sources
Beta strandi133 – 1419Combined sources
Helixi150 – 1534Combined sources
Helixi157 – 1593Combined sources
Beta strandi161 – 17818Combined sources
Beta strandi181 – 1888Combined sources
Turni189 – 1924Combined sources
Beta strandi193 – 1986Combined sources
Beta strandi208 – 2114Combined sources
Helixi214 – 2196Combined sources
Helixi222 – 23211Combined sources
Helixi249 – 25911Combined sources
Beta strandi262 – 2654Combined sources
Beta strandi275 – 2773Combined sources
Turni278 – 2814Combined sources
Helixi282 – 29211Combined sources
Beta strandi295 – 2973Combined sources
Beta strandi299 – 3024Combined sources
Helixi303 – 3053Combined sources
Beta strandi317 – 3204Combined sources
Helixi322 – 33312Combined sources
Turni334 – 3363Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BK4X-ray2.30A2-338[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00637.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 1254Substrate bindingBy similarity
Regioni213 – 2164Substrate bindingBy similarity
Regioni244 – 2496Substrate bindingBy similarity
Regioni275 – 2773Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the FBPase class 1 family.Curated

Phylogenomic databases

HOGENOMiHOG000191265.
HOVERGENiHBG005627.
InParanoidiP00637.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
InterProiIPR000146. FBPase_class-1.
IPR033391. FBPase_N.
IPR028343. FBPtase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERiPTHR11556. PTHR11556. 1 hit.
PfamiPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFiPIRSF500210. FBPtase. 1 hit.
PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSiPR00115. F16BPHPHTASE.
PROSITEiPS00124. FBPASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00637-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADKAPFDTD ISTMTRFVME EGRKAGGTGE MTQLLNSLCT AVKAISTAVR
60 70 80 90 100
KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED
110 120 130 140 150
KNAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSIGTIFGIY RKKSTDEPST
160 170 180 190 200
KDALQPGRNL VAAGYALYGS ATMLVLAGGS GVNSFMLDPA IGEFILVDKN
210 220 230 240 250
VKIKKKGNIY SLNEGYAKDF DPAVTEYIQK KKFPPDNSSP YGARYVGSMV
260 270 280 290 300
ADVHRTLVYG GIFLYPANKK SPDGKLRLLY ECNPMAFIME KAGGMATTGK
310 320 330
EAILDIVPTD IHQRAPVILG SPDDVQEFLE IYKKHAVK
Length:338
Mass (Da):36,578
Last modified:November 24, 2009 - v4
Checksum:i2676BF5964461250
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841N → D AA sequence (PubMed:6289748).Curated
Sequence conflicti89 – 891S → A AA sequence (PubMed:6289748).Curated
Sequence conflicti93 – 931C → S AA sequence (PubMed:6289748).Curated
Sequence conflicti116 – 1172VC → SN AA sequence (PubMed:6289748).Curated
Sequence conflicti122 – 1232DG → VP AA sequence (PubMed:6289748).Curated
Sequence conflicti268 – 2681N → D AA sequence (PubMed:6284034).Curated
Sequence conflicti281 – 2811E → Q AA sequence (PubMed:6284034).Curated
Sequence conflicti284 – 2841Missing AA sequence (PubMed:6284034).Curated
Sequence conflicti301 – 3011E → Q AA sequence (PubMed:6284034).Curated
Sequence conflicti308 – 3136PTDIHQ → QTPDH AA sequence (PubMed:6284034).Curated
Sequence conflicti327 – 3271E → Q AA sequence (PubMed:6284034).Curated
Sequence conflicti330 – 3312Missing AA sequence (PubMed:6284034).Curated

Sequence databases

PIRiS70469.
UniGeneiOcu.3240.

Cross-referencesi

Sequence databases

PIRiS70469.
UniGeneiOcu.3240.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BK4X-ray2.30A2-338[»]
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP00637.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOGENOMiHOG000191265.
HOVERGENiHBG005627.
InParanoidiP00637.

Enzyme and pathway databases

UniPathwayiUPA00138.
SABIO-RKP00637.

Miscellaneous databases

EvolutionaryTraceiP00637.

Family and domain databases

HAMAPiMF_01855. FBPase_class1.
InterProiIPR000146. FBPase_class-1.
IPR033391. FBPase_N.
IPR028343. FBPtase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERiPTHR11556. PTHR11556. 1 hit.
PfamiPF00316. FBPase. 1 hit.
[Graphical view]
PIRSFiPIRSF500210. FBPtase. 1 hit.
PIRSF000904. FBPtase_SBPase. 1 hit.
PRINTSiPR00115. F16BPHPHTASE.
PROSITEiPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19, ACETYLATION AT ALA-2.
    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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 249-289 AND 296-338.
    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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.

Entry informationi

Entry nameiF16P1_RABIT
AccessioniPrimary (citable) accession number: P00637
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 24, 2009
Last modified: June 8, 2016
This is version 121 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.