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Q56815 (ALF_XANFL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 63. 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:cbbA
OrganismXanthobacter flavus
Taxonomic identifier281 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeXanthobacter

Protein attributes

Sequence length354 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 biosynthesis; Calvin cycle.

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 processCalvin cycle
Glycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

reductive pentose-phosphate cycle

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 – 354354Fructose-bisphosphate aldolase
PRO_0000178755

Regions

Region233 – 2353Dihydroxyacetone phosphate binding By similarity
Region275 – 2784Dihydroxyacetone phosphate binding By similarity

Sites

Active site831Proton donor By similarity
Metal binding841Zinc 1; catalytic By similarity
Metal binding1051Zinc 2 By similarity
Metal binding1421Zinc 2 By similarity
Metal binding1981Zinc 1; catalytic By similarity
Metal binding2321Zinc 1; catalytic By similarity
Binding site501Glyceraldehyde 3-phosphate By similarity
Binding site1991Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q56815 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: DDF44661B527E4B7

FASTA35437,982
        10         20         30         40         50         60 
MALVSMRQLL DHAADDSYGL PAFNVNNMEQ VKAIMDAARA TSSPVILQGS AGARKYAGEP 

        70         80         90        100        110        120 
FLRHLIAAAV EAYPEIPVVM HQDHGASPAV CMGAIKSGFS SVMMDGSLKE DGKTPADYDY 

       130        140        150        160        170        180 
NVSVTAKVVE LAHAVGVSVE GELGCLGSLE TGKGEAEDGH GAEEALDHSK LLTDPDEAAQ 

       190        200        210        220        230        240 
FVKATQCDAL AIAIGTSHGA YKFTRKPTGD ILAIDRIKAI HQRIPTTHLV MHGSSSVPQE 

       250        260        270        280        290        300 
LLEEIRTYGG DIKETYGVPV EEIQEGIRYG VRKVNIDTDI RLAMTAAIRR VGAKNKSEFD 

       310        320        330        340        350 
PRKFMAAAME EAKKVCIARF EAFGSAGKAE KIRAIELDEM AKRYASGELA QVVH 

« Hide

References

[1]"Primary structure and phylogeny of the Calvin cycle enzymes transketolase and fructosebisphosphate aldolase of Xanthobacter flavus."
van den Bergh E.R., Baker S.C., Raggers R.J., Terpstra P., Woudstra E.C., Dijkhuizen L., Meijer W.G.
J. Bacteriol. 178:888-893(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: H4-14.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U29134 Genomic DNA. Translation: AAA96742.1.

3D structure databases

ProteinModelPortalQ56815.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00109; UER00183.
UPA00116.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR006412. Fruct_bisP_Calv.
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.
TIGR01521. FruBisAldo_II_B. 1 hit.
PROSITEPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF_XANFL
AccessionPrimary (citable) accession number: Q56815
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 63 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