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Protein

Fructose-1,6-bisphosphate aldolase/phosphatase

Gene

fbp

Organism
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
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

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:MTBMA_c02650Imported
OrganismiMethanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri79929 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000000345 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004371821 – 365Fructose-1,6-bisphosphate aldolase/phosphataseAdd BLAST365

Interactioni

Subunit structurei

Homooctamer; dimer of tetramers.By similarity

Protein-protein interaction databases

STRINGi79929.MTBMA_c02650.

Structurei

3D structure databases

SMRiD9PUH5.
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.
OrthoDBiPOG093Z0396.

Family and domain databases

HAMAPiMF_02067. FBP_aldolase_phosphatase. 1 hit.
InterProiView protein in InterPro
IPR002803. FBPase_V.
IPR036076. FBPase_V_sf.
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.

D9PUH5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTTISVIKA DVGSVAGHAV AHEALKKKCD EILAEARDTG ILEDYYITNC
60 70 80 90 100
GDDIDLIMTH RNGEENEEVH QTAWNAFREA TEVARGLKLY GAGQDLLSDT
110 120 130 140 150
FSGNIKGMGP GCAEMEFKER PSDPVIIFCC DKTEPGAFNL PLFRMFADPF
160 170 180 190 200
NTAGLVIDPT LHNGYEFEVF DVVEHKKVTM ACPDEMYDLL ALLGSISRYV
210 220 230 240 250
IKKIHRRDDG EIAASVSTER LNLMAGKYIG KDDPVAIVRA QSGFPAAGEV
260 270 280 290 300
VEPFAFPHLV GGWMRGSHNG PLMPVAQRDA TPVRFDGPPR VIGLGFQIAD
310 320 330 340 350
CKLVGPIDMF DDPSFDRSRQ LASEIAEYMR RHGPFEPHRL PSDEMEYTSL
360
PGVLEKLGDR FEDMD
Length:365
Mass (Da):40,387
Last modified:October 5, 2010 - v1
Checksum:i52268C30E96934C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001710 Genomic DNA. Translation: ADL57873.1.
RefSeqiWP_013295100.1. NC_014408.1.

Genome annotation databases

EnsemblBacteriaiADL57873; ADL57873; MTBMA_c02650.
GeneIDi9703971.
KEGGimmg:MTBMA_c02650.
PATRICifig|79929.8.peg.259.

Similar proteinsi

Entry informationi

Entry nameiFBPAP_METTM
AccessioniPrimary (citable) accession number: D9PUH5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 7, 2016
Last sequence update: October 5, 2010
Last modified: October 25, 2017
This is version 34 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families