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Protein

Fructose-bisphosphate aldolase class 2

Gene

fba

Organism
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. Is required for the utilization of fructose as a sole carbon and energy source. Plays a role in gluconeogenesis during growth on acetate, D-xylose, and casamino acids.1 Publication

Catalytic activityi

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.1 Publication

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit. One is catalytic and the other provides a structural contribution.By similarity

Enzyme regulationi

EDTA is an inhibitor of catalytic activity.1 Publication

Kineticsi

  1. KM=0.24 mM for D-fructose 1,6-bisphosphate1 Publication
  1. Vmax=55 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 7.5.1 Publication

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Probable glucose-6-phosphate isomerase (pgi), Probable glucose-6-phosphate isomerase (pgi)
  3. no protein annotated in this organism
  4. Fructose-bisphosphate aldolase class 2 (fba)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei53Glyceraldehyde 3-phosphateBy similarity1
Active sitei92Proton donorBy similarity1
Metal bindingi93Zinc 1; catalyticBy similarity1
Metal bindingi115Zinc 2By similarity1
Metal bindingi145Zinc 2By similarity1
Metal bindingi191Zinc 1; catalyticBy similarity1
Binding sitei192Dihydroxyacetone phosphate; via amide nitrogenBy similarity1
Metal bindingi225Zinc 1; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processGlycolysis
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.1.2.13. 2561.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase class 2 (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Fructose-bisphosphate aldolase class II
Gene namesi
Name:fba
Ordered Locus Names:HVO_1494
ORF Names:C498_11261
OrganismiHaloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Taxonomic identifieri309800 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHaloferacalesHaloferacaceaeHaloferax
Proteomesi
  • UP000011532 Componenti: Unassembled WGS sequence
  • UP000008243 Componenti: Chromosome

Pathology & Biotechi

Disruption phenotypei

Loss of growth on fructose, but growth on glucose is slightly stimulated. Loss of growth on acetate, D-xylose, or Casamino acids.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004289811 – 330Fructose-bisphosphate aldolase class 2Add BLAST330

Expressioni

Inductioni

Expression is highly up-regulated in presence of fructose.1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi309800.HVO_1494.

Structurei

3D structure databases

ProteinModelPortaliD4GYE0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni226 – 228Dihydroxyacetone phosphate bindingBy similarity3
Regioni247 – 250Dihydroxyacetone phosphate bindingBy similarity4

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG07500. Archaea.
COG0191. LUCA.
HOGENOMiHOG000227793.
KOiK01624.
OMAiELCKDCI.
OrthoDBiPOG093Z04GN.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR000771. FBA_II.
PfamiView protein in Pfam
PF01116. F_bP_aldolase. 1 hit.
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.

Sequencei

Sequence statusi: Complete.

D4GYE0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFYGGEELA TVYDEALDEG FGLIASNIAE PNIMMGLMEG ADRMDSDLLL
60 70 80 90 100
QMSGGACRFA GDGDAVAGLK AMGNYIETIA ERYDIGVFLN MDHQTDLEFI
110 120 130 140 150
EQQIELDIPS SIMIDASHEP FDENVATSRE VVEMVEAAGS DVLIEAELGQ
160 170 180 190 200
IKGVEDEIEA EEAFYTDPEQ AVEFVDKTGA DLLAISVGTQ HGVAKGKDLE
210 220 230 240 250
LRPDLANDIR QALRDHGLDT PLVLHGSSGV QPDQLQEMLK HGICKVNKDT
260 270 280 290 300
RYQYEYTRTA YDRYNEEPNA IVPPEGVADA RDTFFNETDW SPNKDVFDPR
310 320 330
VAGRDIRERI ADVHADLTEV SGSAGQSLFK
Length:330
Mass (Da):36,302
Last modified:May 18, 2010 - v1
Checksum:i6CF4C55B24F75CD1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001956 Genomic DNA. Translation: ADE02710.1.
AOHU01000090 Genomic DNA. Translation: ELY28268.1.
RefSeqiWP_004043441.1. NZ_AOHU01000090.1.

Genome annotation databases

EnsemblBacteriaiADE02710; ADE02710; HVO_1494.
ELY28268; ELY28268; C498_11261.
GeneIDi8924997.
KEGGihvo:HVO_1494.
PATRICifig|309800.29.peg.2146.

Similar proteinsi

Entry informationi

Entry nameiALF_HALVD
AccessioniPrimary (citable) accession number: D4GYE0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 14, 2014
Last sequence update: May 18, 2010
Last modified: October 25, 2017
This is version 43 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, Reference proteome

Documents

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