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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)DescriptionActionsGraphical viewLength
Metal bindingi69Magnesium 1By similarity1
Metal bindingi98Magnesium 1By similarity1
Metal bindingi98Magnesium 21
Metal bindingi119Magnesium 21
Metal bindingi119Magnesium 3By similarity1
Metal bindingi121Magnesium 2; via carbonyl oxygenBy similarity1
Metal bindingi122Magnesium 3By similarity1
Binding sitei141AMPBy similarity1
Binding sitei265SubstrateBy similarity1
Metal bindingi281Magnesium 3By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 22AMPBy similarity5
Nucleotide bindingi28 – 32AMPBy similarity5
Nucleotide bindingi113 – 114AMPBy similarity2

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00002005012 – 338Fructose-1,6-bisphosphatase 1Add BLAST337

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei151N6-succinyllysineBy similarity1
Modified residuei216PhosphotyrosineBy similarity1
Modified residuei245PhosphotyrosineBy similarity1
Modified residuei265PhosphotyrosineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP00637.

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

Secondary structure

1338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 25Combined sources12
Helixi30 – 49Combined sources20
Turni50 – 53Combined sources4
Helixi74 – 88Combined sources15
Beta strandi92 – 97Combined sources6
Helixi108 – 110Combined sources3
Beta strandi111 – 122Combined sources12
Helixi126 – 129Combined sources4
Beta strandi133 – 141Combined sources9
Helixi150 – 153Combined sources4
Helixi157 – 159Combined sources3
Beta strandi161 – 178Combined sources18
Beta strandi181 – 188Combined sources8
Turni189 – 192Combined sources4
Beta strandi193 – 198Combined sources6
Beta strandi208 – 211Combined sources4
Helixi214 – 219Combined sources6
Helixi222 – 232Combined sources11
Helixi249 – 259Combined sources11
Beta strandi262 – 265Combined sources4
Beta strandi275 – 277Combined sources3
Turni278 – 281Combined sources4
Helixi282 – 292Combined sources11
Beta strandi295 – 297Combined sources3
Beta strandi299 – 302Combined sources4
Helixi303 – 305Combined sources3
Beta strandi317 – 320Combined sources4
Helixi322 – 333Combined sources12
Turni334 – 336Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BK4X-ray2.30A2-338[»]
SMRiP00637.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00637.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni122 – 125Substrate bindingBy similarity4
Regioni213 – 216Substrate bindingBy similarity4
Regioni244 – 249Substrate bindingBy similarity6
Regioni275 – 277Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the FBPase class 1 family.Curated

Phylogenomic databases

HOGENOMiHOG000191265.
HOVERGENiHBG005627.
InParanoidiP00637.

Family and domain databases

CDDicd00354. FBPase. 1 hit.
HAMAPiMF_01855. FBPase_class1. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti84N → D AA sequence (PubMed:6289748).Curated1
Sequence conflicti89S → A AA sequence (PubMed:6289748).Curated1
Sequence conflicti93C → S AA sequence (PubMed:6289748).Curated1
Sequence conflicti116 – 117VC → SN AA sequence (PubMed:6289748).Curated2
Sequence conflicti122 – 123DG → VP AA sequence (PubMed:6289748).Curated2
Sequence conflicti268N → D AA sequence (PubMed:6284034).Curated1
Sequence conflicti281E → Q AA sequence (PubMed:6284034).Curated1
Sequence conflicti284Missing AA sequence (PubMed:6284034).Curated1
Sequence conflicti301E → Q AA sequence (PubMed:6284034).Curated1
Sequence conflicti308 – 313PTDIHQ → QTPDH AA sequence (PubMed:6284034).Curated6
Sequence conflicti327E → Q AA sequence (PubMed:6284034).Curated1
Sequence conflicti330 – 331Missing AA sequence (PubMed:6284034).Curated2

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BK4X-ray2.30A2-338[»]
SMRiP00637.
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

CDDicd00354. FBPase. 1 hit.
HAMAPiMF_01855. FBPase_class1. 1 hit.
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...

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: November 2, 2016
This is version 124 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.