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Protein

Fructose-1,6-bisphosphate aldolase/phosphatase

Gene

fbp

Organism
Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 / 345-15)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P).UniRule annotation

Catalytic activityi

D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.UniRule annotation
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.UniRule annotation

Cofactori

Mg2+UniRule annotation

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.UniRule annotation
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
Active sitei16Proton acceptor; for FBP phosphatase activityUniRule annotation1
Metal bindingi16Magnesium 1UniRule annotation1
Metal bindingi23Magnesium 1; via pros nitrogenUniRule annotation1
Binding sitei23FBP; via tele nitrogenUniRule annotation1
Metal bindingi57Magnesium 1UniRule annotation1
Metal bindingi57Magnesium 2UniRule annotation1
Metal bindingi58Magnesium 2UniRule annotation1
Binding sitei95FBPUniRule annotation1
Metal bindingi99Magnesium 1UniRule annotation1
Metal bindingi136Magnesium 2UniRule annotation1
Binding sitei137FBP/DHAPUniRule annotation1
Active sitei232Proton donor/acceptor; for FBP aldolase activityUniRule annotation1
Active sitei235Schiff-base intermediate with DHAP; for FBP aldolase activityUniRule annotation1
Metal bindingi235Magnesium 3; via carbonyl oxygenUniRule annotation1
Metal bindingi236Magnesium 3UniRule annotation1
Metal bindingi236Magnesium 4UniRule annotation1
Metal bindingi237Magnesium 2UniRule annotation1
Metal bindingi237Magnesium 3UniRule annotation1
Binding sitei269FBP/DHAP; via amide nitrogenUniRule annotation1
Binding sitei290FBP/DHAPUniRule annotation1
Binding sitei351FBPUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolaseUniRule annotation, LyaseUniRule annotation
Biological processCarbohydrate metabolismUniRule annotation, GluconeogenesisUniRule annotation
LigandMagnesiumUniRule annotation, Metal-bindingUniRule annotation, Schiff baseUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-1,6-bisphosphate aldolase/phosphataseUniRule annotation (EC:3.1.3.11UniRule annotation, EC:4.1.2.13UniRule annotation)
Short name:
FBP A/PUniRule annotation
Short name:
FBP aldolase/phosphataseUniRule annotation
Gene namesi
Name:fbpUniRule annotation
Ordered Locus Names:ASAC_1229Imported
OrganismiAcidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 / 345-15)Imported
Taxonomic identifieri666510 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiAcidilobalesAcidilobaceaeAcidilobus
Proteomesi
  • UP000000346 Componenti: Chromosome

Interactioni

Subunit structurei

Homooctamer; dimer of tetramers.UniRule annotation

Protein-protein interaction databases

STRINGi666510.ASAC_1229.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni108 – 109FBP bindingUniRule annotation2
Regioni245 – 246FBP binding; shared with dimeric partnerUniRule annotation2

Domaini

Consists of a single catalytic domain, but remodels its active-site architecture via a large structural change to exhibit dual activities.UniRule annotation

Sequence similaritiesi

Belongs to the FBP aldolase/phosphatase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG04180. Archaea.
COG1980. LUCA.
HOGENOMiHOG000229394.
KOiK01622.
OMAiHLVAGWM.
OrthoDBiPOG093Z0396.

Family and domain databases

HAMAPiMF_02067. FBP_aldolase_phosphatase. 1 hit.
InterProiView protein in InterPro
IPR002803. FBPase_V.
PfamiView protein in Pfam
PF01950. FBPase_3. 1 hit.
PIRSFiPIRSF015647. FBPtase_archl. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD014260. FBPase_V. 1 hit.
SUPFAMiSSF111249. SSF111249. 1 hit.

Sequencei

Sequence statusi: Complete.

D9Q2U6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSGGTKTTL SVIKADIGSI AGHHKAHPDT LLAASRVLAE GKKKGIIADF
60 70 80 90 100
YVTAIGDDIQ LIMTHFRGVN DPQVHELAWS AFKEATSVAK DLGLYAAGQD
110 120 130 140 150
LLSDTFSGNV RGLGPGVAEL EFNERPSEPV AIFMADKTEP SAFNLPLYKI
160 170 180 190 200
FADPFNTAGL VIDPKMHSGF VFTVLDLYEG KAVDLSTPEE LYDLLALIGT
210 220 230 240 250
TSRYVIKYVH RKDGEPAAVV SSERLNLIAG KYIGKDDPVM IVRLQSGFPA
260 270 280 290 300
LGEALEAFSF PHLVAGWMRG SHFGPLMPVG LKDAKMTRFD GPPRVLGLGF
310 320 330 340 350
NIKAGRLVGP TDLFDDVAFD EVRRQAAEIA DYMRRHGPFM PHRLGPEEME
360 370 380
YTTLPDVLKR LEGRFRPFDL GYRPIVKHED LLE
Length:383
Mass (Da):42,025
Last modified:October 5, 2010 - v1
Checksum:i7A2FAF4AB620BA82
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001742 Genomic DNA. Translation: ADL19634.1.

Genome annotation databases

EnsemblBacteriaiADL19634; ADL19634; ASAC_1229.
KEGGiasc:ASAC_1229.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001742 Genomic DNA. Translation: ADL19634.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi666510.ASAC_1229.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADL19634; ADL19634; ASAC_1229.
KEGGiasc:ASAC_1229.

Phylogenomic databases

eggNOGiarCOG04180. Archaea.
COG1980. LUCA.
HOGENOMiHOG000229394.
KOiK01622.
OMAiHLVAGWM.
OrthoDBiPOG093Z0396.

Enzyme and pathway databases

UniPathwayiUPA00138.

Family and domain databases

HAMAPiMF_02067. FBP_aldolase_phosphatase. 1 hit.
InterProiView protein in InterPro
IPR002803. FBPase_V.
PfamiView protein in Pfam
PF01950. FBPase_3. 1 hit.
PIRSFiPIRSF015647. FBPtase_archl. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD014260. FBPase_V. 1 hit.
SUPFAMiSSF111249. SSF111249. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiD9Q2U6_ACIS3
AccessioniPrimary (citable) accession number: D9Q2U6
Entry historyiIntegrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: May 10, 2017
This is version 30 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.