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Protein

Fructose-1,6-bisphosphate aldolase/phosphatase

Gene

fbp

Organism
Cenarchaeum symbiosum (strain A)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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).1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 Publication

Kineticsi

The aldolase reaction is a classic case for a fully reversible enzymatic reaction but here, the KM values for the substrate for the aldol condensation and the aldol cleavage differ by a factor of 1000, and the intrinsic phosphatase activity renders the process irreversible.1 Publication
  1. KM=40 µM for D-fructose 1,6-bisphosphate (when assaying the FBP phosphatase activity, at 48 degrees Celsius)1 Publication
  2. KM=110 µM for triosephosphates (when assaying the FBP aldolase activity in the anabolic direction, at 48 degrees Celsius)1 Publication
  3. KM=100 mM for D-fructose 1,6-bisphosphate (when assaying the FBP aldolase activity in the catabolic direction, at 48 degrees Celsius)1 Publication
  1. Vmax=0.22 µmol/min/mg enzyme for the FBP phosphatase activity (at 48 degrees Celsius)1 Publication
  2. Vmax=0.24 µmol/min/mg enzyme for the FBP aldolase activity in the anabolic direction (at 48 degrees Celsius)1 Publication
  3. Vmax=0.29 µmol/min/mg enzyme for the FBP aldolase activity in the catabolic direction (at 48 degrees Celsius)1 Publication

Temperature dependencei

Heat-stabile at 70 degrees Celsius. Displays a half-life of 20 minutes at 82 degrees Celsius.1 Publication

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.1 Publication
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 sitei11Proton acceptor; for FBP phosphatase activityBy similarity1
Metal bindingi11Magnesium 1By similarity1
Metal bindingi18Magnesium 1; via pros nitrogenBy similarity1
Binding sitei18FBP; via tele nitrogenBy similarity1
Metal bindingi49Magnesium 1By similarity1
Metal bindingi49Magnesium 2By similarity1
Metal bindingi50Magnesium 2By similarity1
Binding sitei87FBPBy similarity1
Metal bindingi91Magnesium 1By similarity1
Metal bindingi128Magnesium 2By similarity1
Binding sitei129FBP/DHAPBy similarity1
Active sitei224Proton donor/acceptor; for FBP aldolase activity1 Publication1
Active sitei227Schiff-base intermediate with DHAP; for FBP aldolase activity1 Publication1
Metal bindingi227Magnesium 3; via carbonyl oxygenBy similarity1
Metal bindingi228Magnesium 3By similarity1
Metal bindingi228Magnesium 4By similarity1
Metal bindingi229Magnesium 2By similarity1
Metal bindingi229Magnesium 3By similarity1
Binding sitei261FBP/DHAP; via amide nitrogenBy similarity1
Binding sitei342FBPBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Lyase, Oxidoreductase
Biological processCarbohydrate metabolism, Gluconeogenesis
LigandMagnesium, Metal-binding, Schiff base

Enzyme and pathway databases

BioCyciCSYM414004:G132A-561-MONOMER
UniPathwayi
UPA00138

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-1,6-bisphosphate aldolase/phosphatase1 Publication (EC:3.1.3.111 Publication, EC:4.1.2.131 Publication)
Short name:
FBP A/PUniRule annotation
Short name:
FBP aldolase/phosphatase1 Publication
Gene namesi
Name:fbpUniRule annotation
Ordered Locus Names:CENSYa_0564Imported
OrganismiCenarchaeum symbiosum (strain A)
Taxonomic identifieri414004 [NCBI]
Taxonomic lineageiArchaeaThaumarchaeotaCenarchaealesCenarchaeaceaeCenarchaeum
Proteomesi
  • UP000000758 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi224Y → F: Shows slightly decreased FBP phosphatase activity, whereas FBP aldolase activity is nearly completely abolished. 1 Publication1
Mutagenesisi227K → R: Shows enhanced FBP phosphatase activity, whereas FBP aldolase activity is completely abolished. 2 Publications1
Mutagenesisi228D → N: Shows completely abolition of both FBP aldolase and FBP phosphatase activities. 1 Publication1
Mutagenesisi341E → Q: Shows unaltered FBP aldolase activity, whereas FBP phosphatase activity is completely abolished. 1 Publication1
Mutagenesisi342Y → F: Shows unaltered FBP aldolase activity, whereas FBP phosphatase activity is completely abolished. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004371791 – 376Fructose-1,6-bisphosphate aldolase/phosphataseAdd BLAST376

Interactioni

Subunit structurei

Homooctamer; dimer of tetramers.By similarity

Structurei

3D structure databases

ProteinModelPortaliA0RV30
SMRiA0RV30
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni100 – 101FBP bindingBy similarity2
Regioni237 – 238FBP binding; shared with dimeric partnerBy similarity2

Domaini

Consists of a single catalytic domain, but remoldels its active-site architecture via a large structural change to exhibit dual activities.By similarity

Sequence similaritiesi

Belongs to the FBP aldolase/phosphatase family.UniRule annotationCurated

Phylogenomic databases

HOGENOMiHOG000229394
KOiK01622

Family and domain databases

HAMAPiMF_02067 FBP_aldolase_phosphatase, 1 hit
InterProiView protein in InterPro
IPR002803 FBPase_V
IPR036076 FBPase_V_sf
PANTHERiPTHR38341 PTHR38341, 1 hit
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.

A0RV30-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRITVSAIKA DVGGIGGHTL PSSGLLDAVR RKVSSSSLLI DHYIGYCGDD
60 70 80 90 100
VHIVMTHTRG TDNSDIHKLA WDAFMEGTRV AKEEGLYGAG QDLLRDSFSG
110 120 130 140 150
NVKGMGPGVA ELEFEERANE AFTVFAADKT EPGAFNYPFY RMFVDSLSNT
160 170 180 190 200
GLIVNKSLAE GVVINIMDVS KARTARLVLW EDKPTIEAAL MYPGRFVVSS
210 220 230 240 250
VETRDGEPIA SASTDRLHNI AGTYVGKDDP ICLVRTQKRF PATEEAGSCF
260 270 280 290 300
NNPHYVAGNT RGSHHMPLMP VRLNSPASIN FCIPIVEALV FSMHEGRLTG
310 320 330 340 350
PFDGFSTPDW DDVRRTATRR AHAMRRQGFV HPATLVPDEL EYAEGYRSRM
360 370
DVLDSKMVPL KDSGPAGTGR AYEDPD
Length:376
Mass (Da):41,145
Last modified:September 7, 2016 - v2
Checksum:iE07465B9739B61E5
GO

Sequence cautioni

The sequence ABK77197 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DP000238 Genomic DNA Translation: ABK77197.1 Different initiation.

Genome annotation databases

EnsemblBacteriaiABK77197; ABK77197; CENSYa_0564
KEGGicsy:CENSYa_0564
PATRICifig|414004.10.peg.513

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DP000238 Genomic DNA Translation: ABK77197.1 Different initiation.

3D structure databases

ProteinModelPortaliA0RV30
SMRiA0RV30
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK77197; ABK77197; CENSYa_0564
KEGGicsy:CENSYa_0564
PATRICifig|414004.10.peg.513

Phylogenomic databases

HOGENOMiHOG000229394
KOiK01622

Enzyme and pathway databases

UniPathwayi
UPA00138

BioCyciCSYM414004:G132A-561-MONOMER

Family and domain databases

HAMAPiMF_02067 FBP_aldolase_phosphatase, 1 hit
InterProiView protein in InterPro
IPR002803 FBPase_V
IPR036076 FBPase_V_sf
PANTHERiPTHR38341 PTHR38341, 1 hit
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 nameiFBPAP_CENSY
AccessioniPrimary (citable) accession number: A0RV30
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 7, 2016
Last sequence update: September 7, 2016
Last modified: October 10, 2018
This is version 49 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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Main funding by: National Institutes of Health

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