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Protein

Fructose-1,6-bisphosphate aldolase/phosphatase

Gene

fbp

Organism
Thermococcus barophilus (strain DSM 11836 / MP)
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 sitei15Proton acceptor; for FBP phosphatase activityUniRule annotation1
Metal bindingi15Magnesium 1UniRule annotation1
Metal bindingi22Magnesium 1; via pros nitrogenUniRule annotation1
Binding sitei22FBP; via tele nitrogenUniRule annotation1
Metal bindingi56Magnesium 1UniRule annotation1
Metal bindingi56Magnesium 2UniRule annotation1
Metal bindingi57Magnesium 2UniRule annotation1
Binding sitei94FBPUniRule annotation1
Metal bindingi98Magnesium 1UniRule annotation1
Metal bindingi135Magnesium 2UniRule annotation1
Binding sitei136FBP/DHAPUniRule annotation1
Active sitei237Proton donor/acceptor; for FBP aldolase activityUniRule annotation1
Active sitei240Schiff-base intermediate with DHAP; for FBP aldolase activityUniRule annotation1
Metal bindingi240Magnesium 3; via carbonyl oxygenUniRule annotation1
Metal bindingi241Magnesium 3UniRule annotation1
Metal bindingi241Magnesium 4UniRule annotation1
Metal bindingi242Magnesium 2UniRule annotation1
Metal bindingi242Magnesium 3UniRule annotation1
Binding sitei274FBP/DHAP; via amide nitrogenUniRule annotation1
Binding sitei295FBP/DHAPUniRule annotation1
Binding sitei357FBPUniRule 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

BioCyciTBAR391623:GH3I-1869-MONOMER.
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:TERMP_01832Imported
OrganismiThermococcus barophilus (strain DSM 11836 / MP)Imported
Taxonomic identifieri391623 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
Proteomesi
  • UP000007478 Componenti: Chromosome

Interactioni

Subunit structurei

Homooctamer; dimer of tetramers.UniRule annotation

Protein-protein interaction databases

STRINGi391623.TERMP_01832.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni107 – 108FBP bindingUniRule annotation2
Regioni250 – 251FBP 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.

F0LKH3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVGEKITIS VIKADIGGWP GHHKVHPALI EKAREILSKA KEEGTIIDFH
60 70 80 90 100
VTYCGDDLQL IMTHKKGTDS PDIHGLAWET FKEATKTAKE LGLYGAGQDL
110 120 130 140 150
LKDAFSGNIR GMGPGAAEME ITIRKSEPIV TFHMDKTEPG AFNLPIFRMF
160 170 180 190 200
ADPFNTAGLV IDPNMHMGFR FEIWDIREHK RVIMNSPEEM YDILALIGAK
210 220 230 240 250
SRYVIKRVFP KEGHKLPKDE PVAVVSTEKL YEIAGEYVGK DDPVAIVRAQ
260 270 280 290 300
SGLPALGEVL EPFAFPHLVS GWMRGSHNGP IMPVPLKYAT PSRFDGPPRA
310 320 330 340 350
VALGWQISPE GKLIGPVDLF DDPAFDWARQ KALEITEYMR RHGPFEPHRL
360 370
PLEEMEYTTL PGVLEKLKDR FEPL
Length:374
Mass (Da):41,824
Last modified:May 3, 2011 - v1
Checksum:i7AB4EF3D0E0E2D09
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002372 Genomic DNA. Translation: ADT84807.1.
RefSeqiWP_013468103.1. NC_014804.1.

Genome annotation databases

EnsemblBacteriaiADT84807; ADT84807; TERMP_01832.
GeneIDi10042148.
KEGGitba:TERMP_01832.
PATRICifig|391623.17.peg.1831.

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.

Entry informationi

Entry nameiF0LKH3_THEBM
AccessioniPrimary (citable) accession number: F0LKH3
Entry historyiIntegrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: June 7, 2017
This is version 27 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported