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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: -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

Caution

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

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

BioCyciHTHE608538:G1GOC-348-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: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
OMAiYMRRHGP
OrthoDBiPOG091H1MW0

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.

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
PATRICifig|608538.5.peg.340

Similar proteinsi

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: March 28, 2018
This is version 47 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported
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Main funding by: National Institutes of Health