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Protein

Fructose-1,6-bisphosphate aldolase/phosphatase

Gene

fbp

Organism
Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6)
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 sitei11Proton acceptor; for FBP phosphatase activityUniRule annotation1
Metal bindingi11Magnesium 1UniRule annotation1
Metal bindingi18Magnesium 1; via pros nitrogenUniRule annotation1
Binding sitei18FBP; via tele nitrogenUniRule annotation1
Metal bindingi52Magnesium 1UniRule annotation1
Metal bindingi52Magnesium 2UniRule annotation1
Metal bindingi53Magnesium 2UniRule annotation1
Binding sitei90FBPUniRule annotation1
Metal bindingi94Magnesium 1UniRule annotation1
Metal bindingi131Magnesium 2UniRule annotation1
Binding sitei132FBP/DHAPUniRule annotation1
Active sitei228Proton donor/acceptor; for FBP aldolase activityUniRule annotation1
Active sitei231Schiff-base intermediate with DHAP; for FBP aldolase activityUniRule annotation1
Metal bindingi231Magnesium 3; via carbonyl oxygenUniRule annotation1
Metal bindingi232Magnesium 3UniRule annotation1
Metal bindingi232Magnesium 4UniRule annotation1
Metal bindingi233Magnesium 2UniRule annotation1
Metal bindingi233Magnesium 3UniRule annotation1
Binding sitei265FBP/DHAP; via amide nitrogenUniRule annotation1
Binding sitei286FBP/DHAPUniRule annotation1
Binding sitei347FBPUniRule annotation1

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:HTH_0340Imported
OrganismiHydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6)Imported
Taxonomic identifieri608538 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeHydrogenobacter
Proteomesi
  • UP000002574 Componenti: Chromosome

Interactioni

Subunit structurei

Homooctamer; dimer of tetramers.UniRule annotation

Protein-protein interaction databases

STRINGi608538.HTH_0340.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni103 – 104FBP bindingUniRule 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

eggNOGiENOG4107NFR. Bacteria.
COG1980. LUCA.
HOGENOMiHOG000229394.
KOiK01622.
OMAiHLVAGWM.
OrthoDBiPOG091H1MW0.

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.

D3DG54-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRITLSVIKA DVGGYVGHSG VHPQLVETIK EFVQEEVKKG ILIDASVLVC
60 70 80 90 100
GDDTAIVMTH THGVDSEIVH GIAWRAFEKA TEVAKKLKLY GAGQDLLSTA
110 120 130 140 150
FSGNVKGMGP GVAEMEFEER PSEPVIVFFA DKTAPSAWNL PLYEMFADPM
160 170 180 190 200
VCAGLVIDPK MHDGFTFEVL DTYTGKAVKL STPSELYELL ALIGTVERYA
210 220 230 240 250
IRSVWRNNDG EIAAVASTQR LSLIAGKYVG KDDPVMVVRA QAGFPAVGEI
260 270 280 290 300
LEPFARPWIV EGWMRGSHNG PLMPVSFKNA TPTRFDGPPR VIAAGYQIAE
310 320 330 340 350
GKLIGPRDLF DDPAFDKARE QAQLMADMLR RQGIFEPHRL PSEEMEYTTL
360 370 380
PKILKKLEER FYELEAPRKA VEDPVEKHDI D
Length:381
Mass (Da):42,113
Last modified:March 23, 2010 - v1
Checksum:iC767693ED30EBE89
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP011112 Genomic DNA. Translation: BAI68806.1.
RefSeqiWP_012962989.1. NC_017161.1.

Genome annotation databases

EnsemblBacteriaiBAI68806; BAI68806; HTH_0340.
KEGGihte:Hydth_0338.
hth:HTH_0340.
PATRICi32209553. VBIHydThe36152_0340.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP011112 Genomic DNA. Translation: BAI68806.1.
RefSeqiWP_012962989.1. NC_017161.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi608538.HTH_0340.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAI68806; BAI68806; HTH_0340.
KEGGihte:Hydth_0338.
hth:HTH_0340.
PATRICi32209553. VBIHydThe36152_0340.

Phylogenomic databases

eggNOGiENOG4107NFR. Bacteria.
COG1980. LUCA.
HOGENOMiHOG000229394.
KOiK01622.
OMAiHLVAGWM.
OrthoDBiPOG091H1MW0.

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 nameiD3DG54_HYDTT
AccessioniPrimary (citable) accession number: D3DG54
Entry historyiIntegrated into UniProtKB/TrEMBL: March 23, 2010
Last sequence update: March 23, 2010
Last modified: April 12, 2017
This is version 40 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation

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.