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P56109 (ALF_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:HP_0176
OrganismHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]
Taxonomic identifier85962 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length307 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete proteome
Reference 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

Chain1 – 307307Fructose-bisphosphate aldolase
PRO_0000178717

Regions

Region211 – 2133Dihydroxyacetone phosphate binding By similarity
Region253 – 2564Dihydroxyacetone phosphate binding By similarity

Sites

Active site821Proton donor By similarity
Metal binding831Zinc 1; catalytic By similarity
Metal binding1041Zinc 2 By similarity
Metal binding1341Zinc 2 By similarity
Metal binding1801Zinc 1; catalytic By similarity
Metal binding2101Zinc 1; catalytic By similarity
Binding site491Glyceraldehyde 3-phosphate By similarity
Binding site1811Dihydroxyacetone phosphate; via amide nitrogen By similarity

Secondary structure

............................................ 307
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56109 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: ADC5696C67C69A45

FASTA30733,773
        10         20         30         40         50         60 
MLVKGNEILL KAHKEGYGVG AFNFVNFEML NAIFEAGNEE NSPLFIQTSE GAIKYMGIDM 

        70         80         90        100        110        120 
AVGMVKTMCE RYPHIPVALH LDHGTTFESC EKAVKAGFTS VMIDASHHAF EENLELTSKV 

       130        140        150        160        170        180 
VKMAHNAGVS VEAELGRLMG IEDNISVDEK DAVLVNPKEA EQFVKESQVD YLAPAIGTSH 

       190        200        210        220        230        240 
GAFKFKGEPK LDFERLQEVK RLTNIPLVLH GASAIPDNVR KSYLDAGGDL KGSKGVPFEF 

       250        260        270        280        290        300 
LQESVKGGIN KVNTDTDLRI AFIAEVRKVA NEDKSQFDLR KFFSPAQLAL KNVVKERMKL 


LGSANKI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000511 Genomic DNA. Translation: AAD07246.1.
PIRH64541.
RefSeqNP_206975.1. NC_000915.1.
YP_006934099.1. NC_018939.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3C4UX-ray1.83A/B1-307[»]
3C52X-ray2.30A/B1-307[»]
3C56X-ray2.30A/B1-307[»]
ProteinModelPortalP56109.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING85962.HP0176.

Chemistry

BindingDBP56109.
ChEMBLCHEMBL1287618.

Proteomic databases

PRIDEP56109.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD07246; AAD07246; HP_0176.
GeneID900140.
KEGGheo:C694_00875.
hpy:HP0176.
PATRIC20591573. VBIHelPyl33062_0186.

Phylogenomic databases

eggNOGCOG0191.
KOK01624.
OMAGKMKETY.
OrthoDBEOG6HXJ7B.

Enzyme and pathway databases

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...

Other

EvolutionaryTraceP56109.

Entry information

Entry nameALF_HELPY
AccessionPrimary (citable) accession number: P56109
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 88 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names