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Q8K9B2 (ALF_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase class 2
Short name=FBP aldolase
Short name=FBPA
EC=4.1.2.13
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Fructose-bisphosphate aldolase class II
Gene names
Name:fbaA
Synonyms:fba
Ordered Locus Names:BUsg_436
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera ›

Protein attributes

Sequence length359 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_processglycolysis

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 – 359359Fructose-bisphosphate aldolase class 2
PRO_0000178709

Regions

Region266 – 2683Dihydroxyacetone phosphate binding By similarity
Region287 – 2904Dihydroxyacetone phosphate binding By similarity

Sites

Active site1101Proton donor By similarity
Metal binding1111Zinc 1; catalytic By similarity
Metal binding1451Zinc 2 By similarity
Metal binding1751Zinc 2 By similarity
Metal binding2271Zinc 1; catalytic By similarity
Metal binding2651Zinc 1; catalytic By similarity
Binding site611Glyceraldehyde 3-phosphate By similarity
Binding site2281Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K9B2 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: F1886D3D05238676

FASTA35940,638
        10         20         30         40         50         60 
MKILNLIQPG VVTGNECQII FELAKKKKFA IPAVNCIGTD SINAVLETAS RVKSPVIIQF 

        70         80         90        100        110        120 
SYGGASFIAG YKRTSSKNPE DQAIQGSISG AQHVHLMSQY YQIPVILHTD HCSKEMLPWI 

       130        140        150        160        170        180 
DGLLEEGKKH YKNFGKPLFT SHMIDLSKEH LKENIAICSN YLKKIKKINM ILEIELGCTG 

       190        200        210        220        230        240 
GEEDGIDNSN IDKKLLYTQP KDVNYAYKKL SKISTNFTIA ASFGNVHGVY QPGNVNLKPN 

       250        260        270        280        290        300 
ILKESQEYVS TKHNLKKLPL NLVFHGGSGS DLKEIHESIE YGIVKMNIDT DIQWASWKGV 

       310        320        330        340        350 
FNFYKKNKDF LQKQIGNKNG KNIPNKKYYD PRSWIRESQE SMSKRLEKTF KDLNAFNIL

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE013218 Genomic DNA. Translation: AAM67979.1.
RefSeqNP_660768.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9B2.
SMRQ8K9B2. Positions 2-359.
ModBaseSearch...

Protein-protein interaction databases

STRING198804.BUsg436.

Proteomic databases

PRIDEQ8K9B2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67979; AAM67979; BUsg_436.
GeneID1005729.
KEGGbas:BUsg436.
PATRIC21247722. VBIBucAph100086_0461.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0191.
KOK01624.
OMAENRFAYP.
ProtClustDBPRK09197.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-481-MONOMER.
UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
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.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF_BUCAP
AccessionPrimary (citable) accession number: Q8K9B2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: May 1, 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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