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Q9PPP3 (ALF_UREPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 80. 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:tsr
Ordered Locus Names:UU596
OrganismUreaplasma parvum serovar 3 (strain ATCC 700970) [Complete proteome] [HAMAP]
Taxonomic identifier273119 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeUreaplasma

Protein attributes

Sequence length290 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.

Subunit structure

Homodimer By similarity.

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 – 290290Fructose-bisphosphate aldolase
PRO_0000178754

Regions

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

Sites

Active site861Proton donor By similarity
Metal binding871Zinc 1; catalytic By similarity
Metal binding1071Zinc 2 By similarity
Metal binding1371Zinc 2 By similarity
Metal binding1791Zinc 1; catalytic By similarity
Metal binding2081Zinc 1; catalytic By similarity
Binding site511Glyceraldehyde 3-phosphate By similarity
Binding site1801Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PPP3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: BD32AB69AE5FE341

FASTA29031,713
        10         20         30         40         50         60 
MSPLVNAKKM IQNAYENHYA VAAININNLE WIKAALLAAQ ETNSPLLLAT SEGAVKYMGG 

        70         80         90        100        110        120 
YDNCYAMVVN LIKQMNIKTP VCLHLDHGTY EGCIKAINAG YSSIMYDGSK LSIEENIKNT 

       130        140        150        160        170        180 
KELLTITKLK GVSVEVEVGS IGGTEDGITS EGELANIDDC YQMCLLDIDM LACGIGNIHG 

       190        200        210        220        230        240 
IYPKNWKGLN FNLLKEINNK VNKPIVLHGG SGISDEQILK AINLGVAKIN INTECQIAFS 

       250        260        270        280        290 
NALQDHLTKA GDLILSKQYD PRKILAYGVD AIKNTIIDKF TKFNSLNKIK 

« Hide

References

[1]"The complete sequence of the mucosal pathogen Ureaplasma urealyticum."
Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y., Cassell G.H.
Nature 407:757-762(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700970.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF222894 Genomic DNA. Translation: AAF31010.1.
RefSeqNP_078435.1. NC_002162.1.

3D structure databases

ProteinModelPortalQ9PPP3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273119.UU596.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF31010; AAF31010; UU596.
GeneID876119.
KEGGuur:UU596.
PATRIC20534829. VBIUrePar45146_0619.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227793.
KOK01624.
OMAMQASQGA.
OrthoDBEOG6HXJ7B.
ProtClustDBCLSK2299005.

Enzyme and pathway databases

BioCycUPAR273119:GHVP-637-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 nameALF_UREPA
AccessionPrimary (citable) accession number: Q9PPP3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 80 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