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Protein

Fructose-bisphosphate aldolase

Gene

fba

Organism
Thermus caldophilus
Status
Reviewed-Annotation score: Annotation score: 3 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.By similarity

Catalytic activityi

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

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 (phi)
  3. ATP-dependent 6-phosphofructokinase (pfk)
  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 sitei49Glyceraldehyde 3-phosphateBy similarity1
Active sitei80Proton donorBy similarity1
Metal bindingi81Zinc 1; catalyticBy similarity1
Metal bindingi102Zinc 2By similarity1
Metal bindingi132Zinc 2By similarity1
Metal bindingi178Zinc 1; catalyticBy similarity1
Binding sitei179Dihydroxyacetone phosphate; via amide nitrogenBy similarity1
Metal bindingi208Zinc 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

BRENDAi4.1.2.13. 6330.
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:fbaImported
OrganismiThermus caldophilus
Taxonomic identifieri272 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001787521 – 305Fructose-bisphosphate aldolaseAdd BLAST305

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1305
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 14Combined sources9
Beta strandi19 – 23Combined sources5
Helixi27 – 38Combined sources12
Helixi39 – 41Combined sources3
Beta strandi44 – 47Combined sources4
Helixi50 – 68Combined sources19
Beta strandi75 – 78Combined sources4
Helixi85 – 93Combined sources9
Beta strandi97 – 101Combined sources5
Helixi108 – 124Combined sources17
Beta strandi128 – 134Combined sources7
Helixi146 – 150Combined sources5
Helixi155 – 164Combined sources10
Beta strandi178 – 181Combined sources4
Beta strandi184 – 186Combined sources3
Helixi191 – 200Combined sources10
Beta strandi205 – 207Combined sources3
Helixi215 – 223Combined sources9
Helixi236 – 244Combined sources9
Beta strandi247 – 252Combined sources6
Helixi254 – 270Combined sources17
Helixi277 – 299Combined sources23

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FJKX-ray2.20A/B/C/D1-305[»]
ProteinModelPortaliQ703I2.
SMRiQ703I2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ703I2.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni209 – 211Dihydroxyacetone phosphate bindingBy similarity3
Regioni251 – 254Dihydroxyacetone 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.

Sequencei

Sequence statusi: Complete.

Q703I2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVTGLEILR KARAEGYGVG AFNTNNMEFT QAILEAAEEM KSPVILALSE
60 70 80 90 100
GAMKYGGRAL TRMVVALAQE ARVPVAVHLD HGSSYESVLK ALREGFTSVM
110 120 130 140 150
IDKSHEDFET NVRETKRVVE AAHAVGVTVE AELGRLAGIE EHVAVDEKDA
160 170 180 190 200
LLTNPEEARI FMERTGADYL AVAIGTSHGA YKGKGRPFID HPRLARIAKL
210 220 230 240 250
VPAPLVLHGA SAVPQELVER FRAAGGEIGE ASGIHPEDIK KAISLGIAKI
260 270 280 290 300
NTDTDLRLAF TALVRETLGK NPKEFDPRKY LGPAREAVKE VVKSRMELFG

SVGRA
Length:305
Mass (Da):32,987
Last modified:July 5, 2004 - v1
Checksum:i9FE260186F29B98A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ621816 Genomic DNA. Translation: CAF32659.1.
AY526903 Genomic DNA. Translation: AAS19362.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ621816 Genomic DNA. Translation: CAF32659.1.
AY526903 Genomic DNA. Translation: AAS19362.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FJKX-ray2.20A/B/C/D1-305[»]
ProteinModelPortaliQ703I2.
SMRiQ703I2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
BRENDAi4.1.2.13. 6330.

Miscellaneous databases

EvolutionaryTraceiQ703I2.

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.
ProtoNetiSearch...

Entry informationi

Entry nameiALF_THECA
AccessioniPrimary (citable) accession number: Q703I2
Secondary accession number(s): P83739
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: July 5, 2004
Last modified: November 30, 2016
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.