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Protein

Fructose-bisphosphate aldolase

Gene

fba

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.By similarity

Catalytic activityi

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

Cofactori

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

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. Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase B (pgiB), Glucose-6-phosphate isomerase A (pgiA), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgiB)
  3. ATP-dependent 6-phosphofructokinase (pfkA), ATP-dependent 6-phosphofructokinase (pfkA), ATP-dependent 6-phosphofructokinase (pfkA), ATP-dependent 6-phosphofructokinase (pfkA)
  4. Fructose-bisphosphate aldolase (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 sitei50Glyceraldehyde 3-phosphateBy similarity1
Active sitei85Proton donorBy similarity1
Metal bindingi86Zinc 1; catalyticBy similarity1
Metal bindingi107Zinc 2By similarity1
Metal bindingi137Zinc 2By similarity1
Metal bindingi181Zinc 1; catalyticBy similarity1
Binding sitei182Dihydroxyacetone phosphate; via amide nitrogenBy similarity1
Metal bindingi209Zinc 1; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene namesi
Name:fba
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001787041 – 287Fructose-bisphosphate aldolaseAdd BLAST287

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei212PhosphothreonineBy similarity1
Modified residuei234PhosphothreonineBy similarity1

Keywords - PTMi

Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliP94453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni210 – 212Dihydroxyacetone phosphate bindingBy similarity3
Regioni231 – 234Dihydroxyacetone phosphate bindingBy similarity4

Sequence similaritiesi

Family and domain databases

CDDicd00947. TBP_aldolase_IIB. 1 hit.
Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000771. FBA_II.
IPR011289. Fruc_bis_ald_class-2.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01859. fruc_bis_ald_. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P94453-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLVSMKEML NEALRGKYAV GQFNINNLEW TQAILAAAEE EKSPVILGVS
60 70 80 90 100
EGAARYMGGF KTVVNMVKGL MEDMNITVPV AIHLDHGSSF EKCKAAIDAG
110 120 130 140 150
FTSVMIDASH HPFEENVRIT SQVVEYAHAR GVSVEAELGI VGGQEDDVVG
160 170 180 190 200
EGVIYADPKE CEELVKRTGI DCLAPALGSV HGPYKGEPKL GFAEMEKIRD
210 220 230 240 250
LTGIPLVLHG GTGIPTEQIQ RAISLGTSKI NVNTENQIAF TKAVRELLAK
260 270 280
DPNVYDPRKI IGPGRDAIKA TVIGKMREFG SSGKAAQ
Length:287
Mass (Da):30,818
Last modified:July 15, 1999 - v3
Checksum:i7D9831D2CEDD07C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11135 Genomic DNA. Translation: CAA72018.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11135 Genomic DNA. Translation: CAA72018.1.

3D structure databases

ProteinModelPortaliP94453.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Family and domain databases

CDDicd00947. TBP_aldolase_IIB. 1 hit.
Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000771. FBA_II.
IPR011289. Fruc_bis_ald_class-2.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01859. fruc_bis_ald_. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALF_GEOSE
AccessioniPrimary (citable) accession number: P94453
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: November 30, 2016
This is version 72 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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

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.