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Protein

Fructose-bisphosphate aldolase class 1

Gene

fbaB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Enzyme regulationi

Activated by citrate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei237 – 2371Schiff-base intermediate with dihydroxyacetone-P

GO - Molecular functioni

  • fructose-bisphosphate aldolase activity Source: UniProtKB-EC
  • identical protein binding Source: IntAct

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase class 1 (EC:4.1.2.13)
Alternative name(s):
Fructose-bisphosphate aldolase class I
Short name:
FBP aldolase
Gene namesi
Name:fbaB
Synonyms:dhnA
Ordered Locus Names:b2097, JW5344
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14062. fbaB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi237 – 2371K → A: Loss of activity.
Mutagenesisi239 – 2391K → A: No change in activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 350349Fructose-bisphosphate aldolase class 1PRO_0000138939Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei208 – 2081N6-acetyllysine1 Publication
Modified residuei262 – 2621N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0A991.
PRIDEiP0A991.

Interactioni

Subunit structurei

Homooctamer or homodecamer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-545269,EBI-545269

Protein-protein interaction databases

DIPiDIP-36197N.
IntActiP0A991. 5 interactions.
STRINGi511145.b2097.

Structurei

3D structure databases

ProteinModelPortaliP0A991.
SMRiP0A991. Positions 70-341.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1830.
HOGENOMiHOG000224791.
InParanoidiP0A991.
KOiK11645.
OMAiIYFGSPE.
OrthoDBiEOG6JQGZX.
PhylomeDBiP0A991.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002915. DeoC/FbaB/lacD_aldolase.
[Graphical view]
PfamiPF01791. DeoC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A991-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDIAQLLGK DADNLLQHRC MTIPSDQLYL PGHDYVDRVM IDNNRPPAVL
60 70 80 90 100
RNMQTLYNTG RLAGTGYLSI LPVDQGVEHS AGASFAANPL YFDPKNIVEL
110 120 130 140 150
AIEAGCNCVA STYGVLASVS RRYAHRIPFL VKLNHNETLS YPNTYDQTLY
160 170 180 190 200
ASVEQAFNMG AVAVGATIYF GSEESRRQIE EISAAFERAH ELGMVTVLWA
210 220 230 240 250
YLRNSAFKKD GVDYHVSADL TGQANHLAAT IGADIVKQKM AENNGGYKAI
260 270 280 290 300
NYGYTDDRVY SKLTSENPID LVRYQLANCY MGRAGLINSG GAAGGETDLS
310 320 330 340 350
DAVRTAVINK RAGGMGLILG RKAFKKSMAD GVKLINAVQD VYLDSKITIA
Length:350
Mass (Da):38,109
Last modified:January 23, 2007 - v2
Checksum:i462341BE2459E587
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti192 – 1921L → V in AAB18249 (Ref. 1) Curated
Sequence conflicti309 – 3091N → I in AAB18249 (Ref. 1) Curated

Mass spectrometryi

Molecular mass is 37979.3 Da from positions 2 - 350. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73760 Genomic DNA. Translation: AAB18249.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75158.2.
AP009048 Genomic DNA. Translation: BAE76584.1.
RefSeqiNP_416600.4. NC_000913.3.
WP_000129551.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC75158; AAC75158; b2097.
BAE76584; BAE76584; BAE76584.
GeneIDi946632.
KEGGieco:b2097.
PATRICi32119527. VBIEscCol129921_2174.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73760 Genomic DNA. Translation: AAB18249.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75158.2.
AP009048 Genomic DNA. Translation: BAE76584.1.
RefSeqiNP_416600.4. NC_000913.3.
WP_000129551.1. NZ_CP010445.1.

3D structure databases

ProteinModelPortaliP0A991.
SMRiP0A991. Positions 70-341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-36197N.
IntActiP0A991. 5 interactions.
STRINGi511145.b2097.

Proteomic databases

PaxDbiP0A991.
PRIDEiP0A991.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75158; AAC75158; b2097.
BAE76584; BAE76584; BAE76584.
GeneIDi946632.
KEGGieco:b2097.
PATRICi32119527. VBIEscCol129921_2174.

Organism-specific databases

EchoBASEiEB3815.
EcoGeneiEG14062. fbaB.

Phylogenomic databases

eggNOGiCOG1830.
HOGENOMiHOG000224791.
InParanoidiP0A991.
KOiK11645.
OMAiIYFGSPE.
OrthoDBiEOG6JQGZX.
PhylomeDBiP0A991.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP0A991.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002915. DeoC/FbaB/lacD_aldolase.
[Graphical view]
PfamiPF01791. DeoC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiALF1_ECOLI
AccessioniPrimary (citable) accession number: P0A991
Secondary accession number(s): P71295, P76416, Q2MAX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.