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P0CZ58 (ALF_STRP3) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase

Short name=FBP aldolase
Short name=FBPA
EC=4.1.2.13
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene names
Name:fba
Ordered Locus Names:SpyM3_1630
OrganismStreptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315) [Complete proteome] [HAMAP]
Taxonomic identifier198466 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length293 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution By similarity.

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processfructose 1,6-bisphosphate metabolic process

Inferred from electronic annotation. Source: InterPro

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 293292Fructose-bisphosphate aldolase
PRO_0000178748

Regions

Region209 – 2113Dihydroxyacetone phosphate binding By similarity
Region230 – 2334Dihydroxyacetone phosphate binding By similarity

Sites

Active site851Proton donor By similarity
Metal binding861Zinc 1; catalytic By similarity
Metal binding1061Zinc 2 By similarity
Metal binding1361Zinc 2 By similarity
Metal binding1781Zinc 1; catalytic By similarity
Metal binding2081Zinc 1; catalytic By similarity
Binding site501Glyceraldehyde 3-phosphate By similarity
Binding site1791Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P0CZ58 [UniParc].

Last modified July 27, 2011. Version 1.
Checksum: B61B3A7C25879D70

FASTA29331,207
        10         20         30         40         50         60 
MAIVSAEKFV QAARKNGYAV GGFNTNNLEW TQAILRAAEA KQAPVLIQTS MGAAKYMGGY 

        70         80         90        100        110        120 
KVCQSLITNL VESMGITVPV AIHLDHGHYE DALECIEVGY TSIMFDGSHL PVEENLAKTA 

       130        140        150        160        170        180 
EVVKIAHAKG VSVEAEVGTI GGEEDGIIGK GELAPIEDAK AMVETGIDFL AAGIGNIHGP 

       190        200        210        220        230        240 
YPENWEGLAL DHLEKLTAAV PGFPIVLHGG SGIPDDQIKE AIRLGVAKVN VNTESQIAFS 

       250        260        270        280        290 
NATREFARNY EANEAEYDGK KLFDPRKFLA PGMKAVQGAV EERIDVFGSA NKA 

« Hide

References

[1]"Genome sequence of a serotype M3 strain of group A Streptococcus: phage-encoded toxins, the high-virulence phenotype, and clone emergence."
Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D., Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S., Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.
Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-595 / MGAS315.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014074 Genomic DNA. Translation: AAM80237.1.
RefSeqNP_665434.1. NC_004070.1.

3D structure databases

ProteinModelPortalP0CZ58.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM80237; AAM80237; SpyM3_1630.
GeneID1009945.
KEGGspg:SpyM3_1630.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000227793.
KOK01624.
OMACTTRYEA.
OrthoDBEOG6HXJ7B.

Enzyme and pathway databases

BioCycSPYO198466:GJDL-1705-MONOMER.
UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR011289. Fruc_bis_ald_class-2.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsTIGR00167. cbbA. 1 hit.
TIGR01859. fruc_bis_ald_. 1 hit.
PROSITEPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF_STRP3
AccessionPrimary (citable) accession number: P0CZ58
Secondary accession number(s): Q8K5W5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 27, 2011
Last modified: June 11, 2014
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways