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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491Glyceraldehyde 3-phosphateBy similarity
Active sitei80 – 801Proton donorBy similarity
Metal bindingi81 – 811Zinc 1; catalyticBy similarity
Metal bindingi102 – 1021Zinc 2By similarity
Metal bindingi132 – 1321Zinc 2By similarity
Metal bindingi178 – 1781Zinc 1; catalyticBy similarity
Binding sitei179 – 1791Dihydroxyacetone phosphate; via amide nitrogenBy similarity
Metal bindingi208 – 2081Zinc 1; catalyticBy similarity

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. fructose 1,6-bisphosphate metabolic process Source: InterPro
  2. glycolytic process Source: UniProtKB-UniPathway
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 305305Fructose-bisphosphate aldolasePRO_0000178752Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1
305
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 149Combined sources
Beta strandi19 – 235Combined sources
Helixi27 – 3812Combined sources
Helixi39 – 413Combined sources
Beta strandi44 – 474Combined sources
Helixi50 – 6819Combined sources
Beta strandi75 – 784Combined sources
Helixi85 – 939Combined sources
Beta strandi97 – 1015Combined sources
Helixi108 – 12417Combined sources
Beta strandi128 – 1347Combined sources
Helixi146 – 1505Combined sources
Helixi155 – 16410Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi184 – 1863Combined sources
Helixi191 – 20010Combined sources
Beta strandi205 – 2073Combined sources
Helixi215 – 2239Combined sources
Helixi236 – 2449Combined sources
Beta strandi247 – 2526Combined sources
Helixi254 – 27017Combined sources
Helixi277 – 29923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FJKX-ray2.20A/B/C/D1-305[»]
ProteinModelPortaliQ703I2.
SMRiQ703I2. Positions 1-305.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ703I2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni209 – 2113Dihydroxyacetone phosphate bindingBy similarity
Regioni251 – 2544Dihydroxyacetone phosphate bindingBy similarity

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR011289. Fruc_bis_ald_class-2.
IPR000771. Ketose_bisP_aldolase_II.
[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
EntryMethodResolution (Å)ChainPositionsPDBsum
2FJKX-ray2.20A/B/C/D1-305[»]
ProteinModelPortaliQ703I2.
SMRiQ703I2. Positions 1-305.
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

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR011289. Fruc_bis_ald_class-2.
IPR000771. Ketose_bisP_aldolase_II.
[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...

Publicationsi

  1. "Crystallization and preliminary X-ray analysis of class II fructose-1,6-bisphosphate aldolase from Thermus caldophilus."
    Lee J.H., Im Y.J., Rho S.-H., Park S.H., Kim M.-K., Cho S.J., Kim T.-Y., Oh J.H., Shin H.-J., Lee D.-S., Eom S.H.
    Protein Pept. Lett. 10:511-515(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

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: April 1, 2015
This is version 52 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

External Data

Dasty 3

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 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.