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Protein

Fructose-1,6-bisphosphate aldolase/phosphatase

Gene

fbp

Organism
Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)
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+By similarity

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 bindingi52Magnesium 1By similarity1
Metal bindingi52Magnesium 2By similarity1
Metal bindingi53Magnesium 2By similarity1
Binding sitei90FBPBy similarity1
Metal bindingi94Magnesium 1By similarity1
Metal bindingi131Magnesium 2By similarity1
Binding sitei132FBP/DHAPBy similarity1
Active sitei228Proton donor/acceptor; for FBP aldolase activityBy similarity1
Active sitei231Schiff-base intermediate with DHAP; for FBP aldolase activityBy similarity1
Metal bindingi231Magnesium 3; via carbonyl oxygenBy similarity1
Metal bindingi232Magnesium 3By similarity1
Metal bindingi232Magnesium 4By similarity1
Metal bindingi233Magnesium 2By similarity1
Metal bindingi233Magnesium 3By similarity1
Binding sitei265FBP/DHAP; via amide nitrogenBy similarity1
Binding sitei286FBP/DHAPBy similarity1
Binding sitei347FBPBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

UniPathwayiUPA00138

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:Msed_2259Imported
OrganismiMetallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)
Taxonomic identifieri399549 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera
Proteomesi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004371811 – 383Fructose-1,6-bisphosphate aldolase/phosphataseAdd BLAST383

Interactioni

Subunit structurei

Homooctamer; dimer of tetramers.By similarity

Protein-protein interaction databases

STRINGi399549.Msed_2259

Structurei

3D structure databases

ProteinModelPortaliA4YIZ5
SMRiA4YIZ5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni103 – 104FBP bindingBy similarity2
Regioni241 – 242FBP binding; shared with dimeric partnerBy similarity2

Domaini

Consists of a single catalytic domain, but remodels 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

eggNOGiarCOG04180 Archaea
COG1980 LUCA
HOGENOMiHOG000229394
KOiK01622
OMAiYMRRHGP
OrthoDBiPOG093Z0396

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.

A4YIZ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSTVSVIKA DIGSLAGHHV VHPDTMAAAN RVLAEAKRQG IILDYYITNV
60 70 80 90 100
GDDLELIMSH TRGELDTKVH ETAWDAFKEA TKVSKELGLY AAGQDLLSDS
110 120 130 140 150
FSGNLKGMGP GIAELDIEER PSEPIAIFMA DKTEPGAFNL PLYKMFADPF
160 170 180 190 200
NTAGLVIDPT MNEGFKFEVL DVYEGQSVVL NSPEEMYSLL GLIGTPARYV
210 220 230 240 250
IRRVYRKADN MIGSVTSIER LNLIAGKYVG KDDPVLIVRL QHGFPALGEA
260 270 280 290 300
LEAFSFPYLV PGWMRGSHYG PIMPVSQRDA KATRFDGPPR LIGLGFNVKN
310 320 330 340 350
GKLTGPSDLF DDPAFDETRR MASVITDYMR RHGPFMPHRL EPTEMEYTTL
360 370 380
PTLIEKLKPR FKKEEDVKKA KPSVYTSKDQ GMD
Length:383
Mass (Da):42,534
Last modified:May 29, 2007 - v1
Checksum:i87D5E21A3CA547C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000682 Genomic DNA Translation: ABP96397.1
RefSeqiWP_012022184.1, NC_009440.1

Genome annotation databases

EnsemblBacteriaiABP96397; ABP96397; Msed_2259
GeneIDi5104211
KEGGimse:Msed_2259

Similar proteinsi

Entry informationi

Entry nameiFBPAP_METS5
AccessioniPrimary (citable) accession number: A4YIZ5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 7, 2016
Last sequence update: May 29, 2007
Last modified: March 28, 2018
This is version 55 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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