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P67478 (ALF2_STAAW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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
Synonyms:fbaA
Ordered Locus Names:MW2049
OrganismStaphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]
Taxonomic identifier196620 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
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

glycolysis

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

Chain1 – 286286Fructose-bisphosphate aldolase
PRO_0000178740

Regions

Region210 – 2123Dihydroxyacetone phosphate binding By similarity
Region231 – 2344Dihydroxyacetone phosphate binding By similarity

Sites

Active site851Proton donor By similarity
Metal binding861Zinc 1; catalytic By similarity
Metal binding1071Zinc 2 By similarity
Metal binding1371Zinc 2 By similarity
Metal binding1811Zinc 1; catalytic By similarity
Metal binding2091Zinc 1; catalytic By similarity
Binding site501Glyceraldehyde 3-phosphate By similarity
Binding site1821Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P67478 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 7A5FD0EBD48283D9

FASTA28630,836
        10         20         30         40         50         60 
MPLVSMKEML IDAKENGYAV GQYNINNLEF TQAILEASQE ENAPVILGVS EGAARYMSGF 

        70         80         90        100        110        120 
YTIVKMVEGL MHDLNITIPV AIHLDHGSSF EKCKEAIDAG FTSVMIDASH SPFEENVATT 

       130        140        150        160        170        180 
KKVVEYAHEK GVSVEAELGT VGGQEDDVVA DGIIYADPKE CQELVEKTGI DALAPALGSV 

       190        200        210        220        230        240 
HGPYKGEPKL GFKEMEEIGL STGLPLVLHG GTGIPTKDIQ KAIPFGTAKI NVNTENQIAS 

       250        260        270        280 
AKAVRDVLNN DKEVYDPRKY LGPAREAIKE TVKGKIKEFG TSNRAK 

« Hide

References

[1]"Genome and virulence determinants of high virulence community-acquired MRSA."
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.
Lancet 359:1819-1827(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MW2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000033 Genomic DNA. Translation: BAB95914.1.
RefSeqNP_646866.1. NC_003923.1.

3D structure databases

ProteinModelPortalP67478.
SMRP67478. Positions 1-285.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196620.MW2049.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB95914; BAB95914; BAB95914.
GeneID1004165.
KEGGsam:MW2049.
PATRIC19570812. VBIStaAur44266_2124.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227793.
KOK01624.
OMAELCKDCI.
OrthoDBEOG6HXJ7B.
ProtClustDBPRK08610.

Enzyme and pathway databases

BioCycSAUR196620:GJ9Z-2118-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.
PROSITEPS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF2_STAAW
AccessionPrimary (citable) accession number: P67478
Secondary accession number(s): Q99SD3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: February 19, 2014
This is version 57 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