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Protein

Fructose-bisphosphate aldolase

Gene

fba

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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)
  3. no protein annotated in this organism
  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 sitei83Proton donorBy similarity1
Metal bindingi84Zinc 1; catalyticBy similarity1
Metal bindingi105Zinc 2By similarity1
Metal bindingi142Zinc 2By similarity1
Metal bindingi198Zinc 1; catalyticBy similarity1
Binding sitei199Dihydroxyacetone phosphate; via amide nitrogenBy similarity1
Metal bindingi232Zinc 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
Synonyms:fda
Ordered Locus Names:PA0555
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA0555.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001787251 – 354Fructose-bisphosphate aldolaseAdd BLAST354

Proteomic databases

PaxDbiQ9I5Y1.
PRIDEiQ9I5Y1.

Interactioni

Protein-protein interaction databases

STRINGi208964.PA0555.

Structurei

3D structure databases

ProteinModelPortaliQ9I5Y1.
SMRiQ9I5Y1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni233 – 235Dihydroxyacetone phosphate bindingBy similarity3
Regioni275 – 278Dihydroxyacetone phosphate bindingBy similarity4

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105D2N. Bacteria.
COG0191. LUCA.
HOGENOMiHOG000227792.
InParanoidiQ9I5Y1.
KOiK01624.
OMAiVNTREMF.
PhylomeDBiQ9I5Y1.

Family and domain databases

CDDicd00947. TBP_aldolase_IIB. 1 hit.
Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000771. FBA_II.
IPR006412. Fruct_bisP_Calv.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01521. FruBisAldo_II_B. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9I5Y1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALISMRQML DHAAEFGYGV PAFNVNNLEQ MRAIMEAADK TDSPVIVQAS
60 70 80 90 100
AGARKYAGAP FLRHLILAAI EEFPHIPVVM HQDHGTSPDV CQRSIQLGFS
110 120 130 140 150
SVMMDGSLRE DGKTPADYDY NVRVTQQTVA FAHACGVSVE GELGCLGSLE
160 170 180 190 200
TGMAGEEDGV GAEGVLDHSQ LLTDPEEAAD FVKKTKVDAL AIAIGTSHGA
210 220 230 240 250
YKFTKPPTGD TLSIQRIKEI HARIPDTHLV MHGSSSVPQD WLAIINEYGG
260 270 280 290 300
EIKETYGVPV EEIVEGIKYG VRKVNIDTDL RLASTGAIRR FLAQNPSEFD
310 320 330 340 350
PRKYFSKTVE AMRDICIARY EAFGTAGNAS KIKPISLEGM FQRYARGELD

PKVN
Length:354
Mass (Da):38,574
Last modified:March 1, 2001 - v1
Checksum:i08864F52A39FC9C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG03944.1.
PIRiC83575.
RefSeqiNP_249246.1. NC_002516.2.
WP_003084964.1. NZ_ASJY01000101.1.

Genome annotation databases

EnsemblBacteriaiAAG03944; AAG03944; PA0555.
GeneIDi880792.
KEGGipae:PA0555.
PATRICi19835372. VBIPseAer58763_0587.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG03944.1.
PIRiC83575.
RefSeqiNP_249246.1. NC_002516.2.
WP_003084964.1. NZ_ASJY01000101.1.

3D structure databases

ProteinModelPortaliQ9I5Y1.
SMRiQ9I5Y1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA0555.

Proteomic databases

PaxDbiQ9I5Y1.
PRIDEiQ9I5Y1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG03944; AAG03944; PA0555.
GeneIDi880792.
KEGGipae:PA0555.
PATRICi19835372. VBIPseAer58763_0587.

Organism-specific databases

PseudoCAPiPA0555.

Phylogenomic databases

eggNOGiENOG4105D2N. Bacteria.
COG0191. LUCA.
HOGENOMiHOG000227792.
InParanoidiQ9I5Y1.
KOiK01624.
OMAiVNTREMF.
PhylomeDBiQ9I5Y1.

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.
IPR006412. Fruct_bisP_Calv.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01521. FruBisAldo_II_B. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALF_PSEAE
AccessioniPrimary (citable) accession number: Q9I5Y1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: March 1, 2001
Last modified: November 30, 2016
This is version 91 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

Complete proteome, Reference proteome

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.