Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P57526 (ALF_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 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:BU451
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]
Taxonomic identifier107806 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length358 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
Reference proteome
Gene Ontology (GO)
   Biological_processglycolytic 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 – 358358Fructose-bisphosphate aldolase class 2
PRO_0000178708

Regions

Region265 – 2673Dihydroxyacetone phosphate binding By similarity
Region286 – 2894Dihydroxyacetone phosphate binding By similarity

Sites

Active site1091Proton donor By similarity
Metal binding1101Zinc 1; catalytic By similarity
Metal binding1441Zinc 2 By similarity
Metal binding1741Zinc 2 By similarity
Metal binding2261Zinc 1; catalytic By similarity
Metal binding2641Zinc 1; catalytic By similarity
Binding site611Glyceraldehyde 3-phosphate By similarity
Binding site2271Dihydroxyacetone phosphate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P57526 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: AB7A47FBF80D2FC2

FASTA35840,663
        10         20         30         40         50         60 
MNILNVIRPG VMNGDEARIV FELAKKKQFA IPAVNCIGTD SINAVLETAA RVKSPIIIQF 

        70         80         90        100        110        120 
SHGGASFIAG YKKKLSENQE QAIQGAVSGA QHVHLMAKHY EIPVILHTDH CPKETLSWID 

       130        140        150        160        170        180 
GLLEVGQNYY FNNNRPLFTS HMIDLSKESL EENISTCKKY FKRIKNINMM LEIELGCTGG 

       190        200        210        220        230        240 
EEDGIDNTKI DKKLLYTQPQ DVNYAYEELN TISKNFSIAA SFGNIHGVYQ PGNIDLRPII 

       250        260        270        280        290        300 
LKNSQEFVSS KHNLEKNPLN LVFHGGSGSN LKEIKESIQY GVVKMNIDTD IQWAAWKGVL 

       310        320        330        340        350 
DFYKQNKEFL QHQLGNTTNK HKPNKKYYDP RTWIRKSQES ISIRLEQSFK ELNSFNIL 

« Hide

References

[1]"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: APS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000003 Genomic DNA. Translation: BAB13149.1.
RefSeqNP_240263.1. NC_002528.1.

3D structure databases

ProteinModelPortalP57526.
SMRP57526. Positions 3-358.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP57526.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB13149; BAB13149; BAB13149.
GeneID1109799.
KEGGbuc:BU451.
PATRIC21244444. VBIBucAph127364_0461.

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227794.
KOK01624.
OMAHNSLDFV.
OrthoDBEOG69GZPB.

Enzyme and pathway databases

BioCycBAPH107806:GBZJ-451-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_BUCAI
AccessionPrimary (citable) accession number: P57526
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: June 11, 2014
This is version 78 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

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names