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Q8CNI3 (ALF2_STAES) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:SE_1723
OrganismStaphylococcus epidermidis (strain ATCC 12228) [Complete proteome] [HAMAP]
Taxonomic identifier176280 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

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: 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_0000178741

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
Q8CNI3 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: D11CBF24BAE3B4E6

FASTA28630,883
        10         20         30         40         50         60 
MPLVSMKEML IDAKENGYAV GQYNLNNLEF TQAILEASQE ENAPVILGVS EGAARYMSGF 

        70         80         90        100        110        120 
YTVVKMVEGL MHDLNITIPV AIHLDHGSSF EKCKEAIDAG FTSVMIDASH SPFEENVEIT 

       130        140        150        160        170        180 
SKVVEYAHDR GVSVEAELGT VGGQEDDVVA DGVIYADPKE CQELVEKTGI DTLAPALGSV 

       190        200        210        220        230        240 
HGPYKGEPKL GFKEMEEIGA STGLPLVLHG GTGIPTKDIQ KAIPYGTAKI NVNTENQIAS 

       250        260        270        280 
AKAVREVLNN DKDVYDPRKY LGPAREAIKE TVKGKIREFG TSNRAK

« Hide

References

[1]"Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228)."
Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.
Mol. Microbiol. 49:1577-1593(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12228.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE015929 Genomic DNA. Translation: AAO05322.1.
RefSeqNP_765278.1. NC_004461.1.

3D structure databases

ProteinModelPortalQ8CNI3.
ModBaseSearch...

Protein-protein interaction databases

STRING176280.SE1723.

Proteomic databases

PRIDEQ8CNI3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO05322; AAO05322; SE_1723.
GeneID1057228.
KEGGsep:SE1723.
PATRIC19609308. VBIStaEpi113981_1683.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0191.
KOK01624.
OMAAIKETVI.
ProtClustDBPRK08610.

Enzyme and pathway databases

BioCycSEPI176280:GCDG-1773-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. False negative.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF2_STAES
AccessionPrimary (citable) accession number: Q8CNI3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: March 1, 2003
Last modified: May 29, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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