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P0A992 (ALF1_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 1

EC=4.1.2.13
Alternative name(s):
Fructose-bisphosphate aldolase class I
Short name=FBP aldolase
Gene names
Name:fbaB
Ordered Locus Names:c2623
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Subunit structure

Homooctamer or homodecamer By similarity.

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the DeoC/FbaB aldolase family. FbaB subfamily.

Sequence caution

The sequence AAN81079.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   PTMAcetylation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 350349Fructose-bisphosphate aldolase class 1
PRO_0000138940

Sites

Active site2371Schiff-base intermediate with dihydroxyacetone-P

Amino acid modifications

Modified residue2081N6-acetyllysine By similarity
Modified residue2621N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A992 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 462341BE2459E587

FASTA35038,109
        10         20         30         40         50         60 
MTDIAQLLGK DADNLLQHRC MTIPSDQLYL PGHDYVDRVM IDNNRPPAVL RNMQTLYNTG 

        70         80         90        100        110        120 
RLAGTGYLSI LPVDQGVEHS AGASFAANPL YFDPKNIVEL AIEAGCNCVA STYGVLASVS 

       130        140        150        160        170        180 
RRYAHRIPFL VKLNHNETLS YPNTYDQTLY ASVEQAFNMG AVAVGATIYF GSEESRRQIE 

       190        200        210        220        230        240 
EISAAFERAH ELGMVTVLWA YLRNSAFKKD GVDYHVSADL TGQANHLAAT IGADIVKQKM 

       250        260        270        280        290        300 
AENNGGYKAI NYGYTDDRVY SKLTSENPID LVRYQLANCY MGRAGLINSG GAAGGETDLS 

       310        320        330        340        350 
DAVRTAVINK RAGGMGLILG RKAFKKSMAD GVKLINAVQD VYLDSKITIA 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN81079.1. Different initiation.
RefSeqNP_754511.2. NC_004431.1.

3D structure databases

ProteinModelPortalP0A992.
SMRP0A992. Positions 49-343.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c2623.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN81079; AAN81079; c2623.
GeneID1037944.
KEGGecc:c2623.
PATRIC18283118. VBIEscCol75197_2467.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000224791.
KOK11645.
OMARYQVLNC.
OrthoDBEOG6JQGZX.
ProtClustDBPRK09250.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR002915. DeoC/FbaB/lacD_aldolase.
[Graphical view]
PfamPF01791. DeoC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF1_ECOL6
AccessionPrimary (citable) accession number: P0A992
Secondary accession number(s): P71295, P76416
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 57 of the entry and version 2 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