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Protein

Fructose-bisphosphate aldolase

Gene

fba

Organism
Staphylococcus aureus (strain MSSA476)
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. ATP-dependent 6-phosphofructokinase (pfkA)
  4. Fructose-bisphosphate aldolase (fba), Fructose-bisphosphate aldolase class 1 (fda)
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
Synonyms:fbaA
Ordered Locus Names:SAS2028
OrganismiStaphylococcus aureus (strain MSSA476)
Taxonomic identifieri282459 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001787391 – 286Fructose-bisphosphate aldolaseAdd BLAST286

Proteomic databases

PRIDEiQ6G7I5.

Structurei

3D structure databases

ProteinModelPortaliQ6G7I5.
SMRiQ6G7I5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000227793.
KOiK01624.
OMAiVNTREMF.

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.
PROSITEiPS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6G7I5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLVSMKEML IDAKENGYAV GQYNINNLEF TQAILEASQE ENAPVILGVS
60 70 80 90 100
EGAARYMSGF YTIVKMVEGL MHDLNITIPV AIHLDHGSSF EKCKEAIDAG
110 120 130 140 150
FTSVMIDASH SPFEENVATT KKVVEYAHEK GVSVEAELGT VGGQEDDVVA
160 170 180 190 200
DGIIYADPKE CQELVEKTGI DALAPALGSV HGPYKGEPKL GFKEMEEIGL
210 220 230 240 250
STGLPLVLHG GTGIPTKDIQ KAIPFGTAKI NVNTENQIAS AKAVRDVLNN
260 270 280
DKEVYDPRKY LGPAREAIKE TVKGKIKEFG TSNRAK
Length:286
Mass (Da):30,836
Last modified:July 19, 2004 - v1
Checksum:i7A5FD0EBD48283D9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571857 Genomic DNA. Translation: CAG43836.1.
RefSeqiWP_001131841.1. NC_002953.3.

Genome annotation databases

GeneIDi28380289.
KEGGisas:SAS2028.
PATRICi19553667. VBIStaAur96780_2110.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571857 Genomic DNA. Translation: CAG43836.1.
RefSeqiWP_001131841.1. NC_002953.3.

3D structure databases

ProteinModelPortaliQ6G7I5.
SMRiQ6G7I5.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ6G7I5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi28380289.
KEGGisas:SAS2028.
PATRICi19553667. VBIStaAur96780_2110.

Phylogenomic databases

HOGENOMiHOG000227793.
KOiK01624.
OMAiVNTREMF.

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.
PROSITEiPS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALF2_STAAS
AccessioniPrimary (citable) accession number: Q6G7I5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: July 19, 2004
Last modified: November 30, 2016
This is version 77 of the entry and version 1 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.