Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P78055 (FSAA_ECOLI)

Last modified November 24, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Fructose-6-phosphate aldolase 1
    EC=4.1.2.-
Gene names
Name: fsaA
Synonyms: fsa, mipB, ybiZ
Ordered Locus Names: b0825, JW5109
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

D-fructose 6-phosphate = glycerone + D-glyceraldehyde 3-phosphate. HAMAP MF_00496

Enzyme regulation

Inhibited by glycerol, inorganic phosphate and arabinose 5-phosphate. HAMAP MF_00496

Subunit structure

Homodecamer or homododecamer. HAMAP MF_00496

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the transaldolase family. Type 3A subfamily.

Mass spectrometry

Molecular mass is 22998 Da from positions 1 - 220. Determined by ESI. Ref.5

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processfructose metabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaldehyde-lyase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 220220Fructose-6-phosphate aldolase 1 HAMAP MF_00496
PRO_0000173643

Sites

Active site851 HAMAP MF_00496

Experimental info

Mutagenesis851K → R: Almost complete loss of activity. Ref.5

Secondary structure

....................................... 220
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P78055-1 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 317B9A06CD19C587

FASTA22022,997
        10         20         30         40         50         60 
MELYLDTSDV VAVKALSRIF PLAGVTTNPS IIAAGKKPLD VVLPQLHEAM GGQGRLFAQV 

        70         80         90        100        110        120 
MATTAEGMVN DALKLRSIIA DIVVKVPVTA EGLAAIKMLK AEGIPTLGTA VYGAAQGLLS 

       130        140        150        160        170        180 
ALAGAEYVAP YVNRIDAQGG SGIQTVTDLH QLLKMHAPQA KVLAASFKTP RQALDCLLAG 

       190        200        210        220 
CESITLPLDV AQQMISYPAV DAAVAKFEQD WQGAFGRTSI 

« Hide

References

« Hide 'large scale' references
[1]Isomura M., Ogino T., Mizuno T.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[2]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"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 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Fructose-6-phosphate aldolase is a novel class I aldolase from Escherichia coli and is related to a novel group of bacterial transaldolases."
Schuermann M., Sprenger G.A.
J. Biol. Chem. 276:11055-11061(2001) [PubMed: 11120740] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10, CHARACTERIZATION, MASS SPECTROMETRY, MUTAGENESIS OF LYS-85.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
+Additional computationally mapped references.

Cross-references

Sequence databases

D88188 Genomic DNA. Translation: BAA13552.1.
U00096 Genomic DNA. Translation: AAC73912.1. Different initiation.
AP009048 Genomic DNA. Translation: BAA35513.2.
PIRA64820.
RefSeqAP_001456.1.
NP_415346.4.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1L6WX-ray1.93A/B/C/D/E/F/G/H/I/J1-220[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:10218N.
STRINGP78055.

Genome annotation databases

GeneID945449.
GenomeReviewsGene locus JW5109 in contig AP009048_GR.
Gene locus b0825 in contig U00096_GR.
KEGGecj:JW5109.
eco:b0825.

Organism-specific databases

EchoBASEEB3244.
EcoGeneEG13471. fsaA.
CMRSearch...

Phylogenomic databases

HOGENOMP78055.
OMAMSAANID

Enzyme and pathway databases

BioCycEcoCyc:G6428-MON.
ECOL168927:B0825-MON.
MetaCyc:G6428-MON.

Gene expression databases

GenevestigatorP78055.

Family and domain databases

HAMAPMF_00496.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR001585. Transaldolase.
IPR018225. Transaldolase_AS.
IPR004731. Transaldolase_C.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR10683. Transaldolase. 1 hit.
PfamPF00923. Transaldolase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00875. talC. 1 hit.
PROSITEPS01054. TRANSALDOLASE_1. 1 hit.
PS00958. TRANSALDOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFSAA_ECOLI
AccessionPrimary (citable) accession number: P78055
Secondary accession number(s): P77855, Q9R3X3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: November 24, 2009
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents