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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: Annotation score: 4 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Lyase

Keywords - Biological processi

Carbohydrate metabolism, Gluconeogenesis

Keywords - Ligandi

Magnesium, Metal-binding, Schiff base

Enzyme and pathway databases

BioCyciMSED399549:GH1O-2264-MONOMER.
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
  • UP000000242 Componenti: Chromosome

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.
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.
OMAiHLVAGWM.

Family and domain databases

HAMAPiMF_02067. FBP_aldolase_phosphatase. 1 hit.
InterProiIPR002803. FBPase_V.
[Graphical view]
PfamiPF01950. FBPase_3. 1 hit.
[Graphical view]
PIRSFiPIRSF015647. FBPtase_archl. 1 hit.
ProDomiPD014260. FBPase_V. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliA4YIZ5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi399549.Msed_2259.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP96397; ABP96397; Msed_2259.
GeneIDi5104211.
KEGGimse:Msed_2259.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00138.
BioCyciMSED399549:GH1O-2264-MONOMER.

Family and domain databases

HAMAPiMF_02067. FBP_aldolase_phosphatase. 1 hit.
InterProiIPR002803. FBPase_V.
[Graphical view]
PfamiPF01950. FBPase_3. 1 hit.
[Graphical view]
PIRSFiPIRSF015647. FBPtase_archl. 1 hit.
ProDomiPD014260. FBPase_V. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF111249. SSF111249. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFBPAP_METS5
AccessioniPrimary (citable) accession number: A4YIZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 7, 2016
Last sequence update: May 29, 2007
Last modified: November 2, 2016
This is version 48 of the entry and version 1 of the sequence. [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

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.