Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fructose-bisphosphate aldolase

Gene

fba

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed-Annotation score: -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.

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

Keywordsi

Molecular functionLyase
Biological processGlycolysis
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathwayi
UPA00109;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:SA1927
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000751 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001787371 – 286Fructose-bisphosphate aldolaseAdd BLAST286

2D gel databases

SWISS-2DPAGEiP99075

Structurei

3D structure databases

ProteinModelPortaliP99075
SMRiP99075
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
OMAiELCKDCI

Family and domain databases

CDDicd00947 TBP_aldolase_IIB, 1 hit
Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR000771 FBA_II
IPR011289 Fruc_bis_ald_class-2
PfamiView protein in Pfam
PF01116 F_bP_aldolase, 1 hit
PIRSFiPIRSF001359 F_bP_aldolase_II, 1 hit
TIGRFAMsiTIGR00167 cbbA, 1 hit
TIGR01859 fruc_bis_ald_, 1 hit
PROSITEiView protein in PROSITE
PS00806 ALDOLASE_CLASS_II_2, 1 hit

Sequencei

Sequence statusi: Complete.

P99075-1 [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:October 11, 2004 - v1
Checksum:i7A5FD0EBD48283D9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA Translation: BAB43211.1
PIRiB90006
RefSeqiWP_001131841.1, NC_002745.2

Genome annotation databases

EnsemblBacteriaiBAB43211; BAB43211; BAB43211
KEGGisau:SA1927

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA Translation: BAB43211.1
PIRiB90006
RefSeqiWP_001131841.1, NC_002745.2

3D structure databases

ProteinModelPortaliP99075
SMRiP99075
ModBaseiSearch...
MobiDBiSearch...

2D gel databases

SWISS-2DPAGEiP99075

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB43211; BAB43211; BAB43211
KEGGisau:SA1927

Phylogenomic databases

HOGENOMiHOG000227793
KOiK01624
OMAiELCKDCI

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00183

Family and domain databases

CDDicd00947 TBP_aldolase_IIB, 1 hit
Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR000771 FBA_II
IPR011289 Fruc_bis_ald_class-2
PfamiView protein in Pfam
PF01116 F_bP_aldolase, 1 hit
PIRSFiPIRSF001359 F_bP_aldolase_II, 1 hit
TIGRFAMsiTIGR00167 cbbA, 1 hit
TIGR01859 fruc_bis_ald_, 1 hit
PROSITEiView protein in PROSITE
PS00806 ALDOLASE_CLASS_II_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiALF2_STAAN
AccessioniPrimary (citable) accession number: P99075
Secondary accession number(s): Q99SD3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: March 28, 2018
This is version 80 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again