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P0A991 (ALF1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 72. 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·Interactions·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
Synonyms:dhnA
Ordered Locus Names:b2097, JW5344
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Enzyme regulation

Activated by citrate.

Subunit structure

Homooctamer or homodecamer.

Subcellular location

Cytoplasm Probable.

Sequence similarities

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

Caution

Was originally (Ref.1) thought to be a dehydrin.

Mass spectrometry

Molecular mass is 37979.3 Da from positions 2 - 350. Determined by MALDI. Ref.4

Sequence caution

The sequence AAB18249.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from direct assay PubMed 16858726. Source: UniProtKB

membrane

Inferred from direct assay PubMed 16858726. Source: UniProtKB

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

identical protein binding

Inferred from physical interaction PubMed 16858726. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-545269,EBI-545269

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 350349Fructose-bisphosphate aldolase class 1
PRO_0000138939

Sites

Active site2371Schiff-base intermediate with dihydroxyacetone-P

Amino acid modifications

Modified residue2081N6-acetyllysine Ref.5
Modified residue2621N6-acetyllysine Ref.5

Experimental info

Mutagenesis2371K → A: Loss of activity.
Mutagenesis2391K → A: No change in activity.
Sequence conflict1921L → V in AAB18249. Ref.1
Sequence conflict3091N → I in AAB18249. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0A991 [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

« Hide 'large scale' references
[1]Close T.J., Choi D.W.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The dhnA gene of Escherichia coli encodes a class I fructose bisphosphate aldolase."
Thomson G.J., Howlett G.J., Ashcroft A.E., Berry A.
Biochem. J. 331:437-445(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-10, CHARACTERIZATION, MASS SPECTROMETRY.
[5]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-208 AND LYS-262, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U73760 Genomic DNA. Translation: AAB18249.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75158.2.
AP009048 Genomic DNA. Translation: BAE76584.1.
RefSeqNP_416600.4. NC_000913.3.
YP_490337.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0A991.
SMRP0A991. Positions 70-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36197N.
IntActP0A991. 5 interactions.
STRING511145.b2097.

Proteomic databases

PaxDbP0A991.
PRIDEP0A991.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75158; AAC75158; b2097.
BAE76584; BAE76584; BAE76584.
GeneID12932531.
946632.
KEGGecj:Y75_p2059.
eco:b2097.
PATRIC32119527. VBIEscCol129921_2174.

Organism-specific databases

EchoBASEEB3815.
EcoGeneEG14062. fbaB.

Phylogenomic databases

eggNOGCOG1830.
HOGENOMHOG000224791.
KOK11645.
OMAQYDQTLY.
OrthoDBEOG6JQGZX.
PhylomeDBP0A991.

Enzyme and pathway databases

BioCycEcoCyc:FRUCBISALD-CLASSI-MONOMER.
ECOL316407:JW5344-MONOMER.
MetaCyc:FRUCBISALD-CLASSI-MONOMER.
SABIO-RKP0A991.

Gene expression databases

GenevestigatorP0A991.

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...

Other

PROP0A991.

Entry information

Entry nameALF1_ECOLI
AccessionPrimary (citable) accession number: P0A991
Secondary accession number(s): P71295, P76416, Q2MAX2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 72 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene