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P0AB71

- ALF_ECOLI

UniProt

P0AB71 - ALF_ECOLI

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Protein
Fructose-bisphosphate aldolase class 2
Gene
fbaA, fba, fda, b2925, JW2892
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution.

Kineticsi

The catalytic efficiency measured with fructose-1,6-bisphosphate as substrate is 1440-fold higher than that with tagatose-1,6-bisphosphate.

  1. KM=0.17 mM for fructose-1,6-bisphosphate1 Publication
  2. KM=0.35 mM for tagatose-1,6-bisphosphate

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621Glyceraldehyde 3-phosphate Inferred
Active sitei110 – 1101Proton donor1 Publication
Metal bindingi111 – 1111Zinc 1; catalytic
Metal bindingi145 – 1451Zinc 2
Metal bindingi175 – 1751Zinc 2
Metal bindingi227 – 2271Zinc 1; catalytic
Binding sitei228 – 2281Dihydroxyacetone phosphate; via amide nitrogen
Metal bindingi265 – 2651Zinc 1; catalytic

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: EcoliWiki
  2. protein binding Source: IntAct
  3. zinc ion binding Source: EcoliWiki

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:FRUCTBISALD-CLASSII-MONOMER.
ECOL316407:JW2892-MONOMER.
MetaCyc:FRUCTBISALD-CLASSII-MONOMER.
SABIO-RKP0AB71.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase class 2 (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Fructose-bisphosphate aldolase class II
Gene namesi
Name:fbaA
Synonyms:fba, fda
Ordered Locus Names:b2925, JW2892
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10282. fbaA.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi36 – 361N → A: 1.5% of wild-type activity. 5-fold decrease in FBP affinity. 1 Publication
Mutagenesisi60 – 601Q → A: 81% of wild-type activity. 1.3-fold decrease in FBP affinity. 1 Publication
Mutagenesisi62 – 621S → A: 8% of wild-type activity. 16-fold decrease in FBP affinity. 1 Publication
Mutagenesisi62 – 621S → T: 60% of wild-type activity. 2.5-fold decrease in FBP affinity. 1 Publication
Mutagenesisi108 – 1081H → A: Loss of activity. 1 Publication
Mutagenesisi111 – 1111H → A: Loss of activity. 1 Publication
Mutagenesisi112 – 1121C → A: Partial loss of activity. 1 Publication
Mutagenesisi326 – 3261K → A: 6% of wild-type activity. 2.2-fold decrease in FBP affinity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 359358Fructose-bisphosphate aldolase class 2
PRO_0000178713Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91N6-acetyllysine; alternate1 Publication
Modified residuei9 – 91N6-malonyllysine; alternate1 Publication
Modified residuei9 – 91N6-succinyllysine; alternate1 Publication
Modified residuei72 – 721N6-succinyllysine1 Publication
Modified residuei115 – 1151N6-succinyllysine1 Publication
Modified residuei231 – 2311N6-succinyllysine1 Publication
Modified residuei251 – 2511N6-succinyllysine1 Publication
Modified residuei319 – 3191N6-succinyllysine1 Publication
Modified residuei326 – 3261N6-succinyllysine1 Publication
Modified residuei348 – 3481N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0AB71.
PRIDEiP0AB71.

2D gel databases

SWISS-2DPAGEP0AB71.

Expressioni

Gene expression databases

GenevestigatoriP0AB71.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
dnaKP0A6Y82EBI-370916,EBI-542092

Protein-protein interaction databases

BioGridi851736. 1 interaction.
DIPiDIP-31872N.
IntActiP0AB71. 7 interactions.
STRINGi511145.b2925.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63
Beta strandi10 – 123
Helixi16 – 2712
Beta strandi32 – 365
Helixi40 – 5314
Beta strandi57 – 615
Helixi63 – 708
Helixi81 – 9717
Helixi98 – 1003
Beta strandi104 – 1096
Helixi114 – 1163
Helixi117 – 13418
Beta strandi140 – 1445
Helixi151 – 16717
Beta strandi171 – 1755
Helixi200 – 21112
Beta strandi217 – 2204
Helixi232 – 2343
Helixi240 – 25314
Beta strandi262 – 2643
Helixi272 – 2809
Beta strandi283 – 2886
Helixi290 – 30718
Helixi308 – 3103
Beta strandi311 – 3177
Beta strandi320 – 3245
Helixi326 – 3294
Helixi331 – 35222

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B57X-ray2.00A/B2-359[»]
1DOSX-ray1.67A/B2-359[»]
1GYNX-ray2.00A2-359[»]
1ZENX-ray2.50A2-359[»]
ProteinModelPortaliP0AB71.
SMRiP0AB71. Positions 2-359.

Miscellaneous databases

EvolutionaryTraceiP0AB71.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni266 – 2683Dihydroxyacetone phosphate binding
Regioni287 – 2904Dihydroxyacetone phosphate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0191.
HOGENOMiHOG000227794.
KOiK01624.
OMAiHNSLDFV.
OrthoDBiEOG69GZPB.
PhylomeDBiP0AB71.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0AB71-1 [UniParc]FASTAAdd to Basket

« Hide

MSKIFDFVKP GVITGDDVQK VFQVAKENNF ALPAVNCVGT DSINAVLETA    50
AKVKAPVIVQ FSNGGASFIA GKGVKSDVPQ GAAILGAISG AHHVHQMAEH 100
YGVPVILHTD HCAKKLLPWI DGLLDAGEKH FAATGKPLFS SHMIDLSEES 150
LQENIEICSK YLERMSKIGM TLEIELGCTG GEEDGVDNSH MDASALYTQP 200
EDVDYAYTEL SKISPRFTIA ASFGNVHGVY KPGNVVLTPT ILRDSQEYVS 250
KKHNLPHNSL NFVFHGGSGS TAQEIKDSVS YGVVKMNIDT DTQWATWEGV 300
LNYYKANEAY LQGQLGNPKG EDQPNKKYYD PRVWLRAGQT SMIARLEKAF 350
QELNAIDVL 359
Length:359
Mass (Da):39,147
Last modified:January 23, 2007 - v2
Checksum:i7A076D9EA62FBEC4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14436 Genomic DNA. Translation: CAA32605.1.
U28377 Genomic DNA. Translation: AAA69092.1.
U00096 Genomic DNA. Translation: AAC75962.1.
AP009048 Genomic DNA. Translation: BAE76989.1.
PIRiS02177. ADEC2A.
RefSeqiNP_417400.1. NC_000913.3.
YP_491125.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75962; AAC75962; b2925.
BAE76989; BAE76989; BAE76989.
GeneIDi12933075.
947415.
KEGGiecj:Y75_p2856.
eco:b2925.
PATRICi32121264. VBIEscCol129921_3020.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14436 Genomic DNA. Translation: CAA32605.1 .
U28377 Genomic DNA. Translation: AAA69092.1 .
U00096 Genomic DNA. Translation: AAC75962.1 .
AP009048 Genomic DNA. Translation: BAE76989.1 .
PIRi S02177. ADEC2A.
RefSeqi NP_417400.1. NC_000913.3.
YP_491125.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B57 X-ray 2.00 A/B 2-359 [» ]
1DOS X-ray 1.67 A/B 2-359 [» ]
1GYN X-ray 2.00 A 2-359 [» ]
1ZEN X-ray 2.50 A 2-359 [» ]
ProteinModelPortali P0AB71.
SMRi P0AB71. Positions 2-359.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 851736. 1 interaction.
DIPi DIP-31872N.
IntActi P0AB71. 7 interactions.
STRINGi 511145.b2925.

Chemistry

BindingDBi P0AB71.
ChEMBLi CHEMBL4912.

2D gel databases

SWISS-2DPAGE P0AB71.

Proteomic databases

PaxDbi P0AB71.
PRIDEi P0AB71.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75962 ; AAC75962 ; b2925 .
BAE76989 ; BAE76989 ; BAE76989 .
GeneIDi 12933075.
947415.
KEGGi ecj:Y75_p2856.
eco:b2925.
PATRICi 32121264. VBIEscCol129921_3020.

Organism-specific databases

EchoBASEi EB0278.
EcoGenei EG10282. fbaA.

Phylogenomic databases

eggNOGi COG0191.
HOGENOMi HOG000227794.
KOi K01624.
OMAi HNSLDFV.
OrthoDBi EOG69GZPB.
PhylomeDBi P0AB71.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .
BioCyci EcoCyc:FRUCTBISALD-CLASSII-MONOMER.
ECOL316407:JW2892-MONOMER.
MetaCyc:FRUCTBISALD-CLASSII-MONOMER.
SABIO-RK P0AB71.

Miscellaneous databases

EvolutionaryTracei P0AB71.
PROi P0AB71.

Gene expression databases

Genevestigatori P0AB71.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view ]
Pfami PF01116. F_bP_aldolase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsi TIGR00167. cbbA. 1 hit.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEi PS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli."
    Alefounder P.R., Perham R.N.
    Mol. Microbiol. 3:723-732(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / CS520.
  2. "Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli."
    Alefounder P.R., Baldwin S.A., Perham R.N., Short N.J.
    Biochem. J. 257:529-534(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-27.
  3. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  6. Cited for: PROTEIN SEQUENCE OF 2-5.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli."
    Berry A., Marshall K.E.
    FEBS Lett. 318:11-16(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-108; HIS-111 AND CYS-112.
  8. "Exploring substrate binding and discrimination in fructose 1,6-bisphosphate and tagatose 1,6-bisphosphate aldolases."
    Zgiby S.M., Thomson G.J., Qamar S., Berry A.
    Eur. J. Biochem. 267:1858-1868(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, REACTION MECHANISM, MUTAGENESIS OF ASN-36; GLN-60; SER-62 AND LYS-326.
    Strain: K12 / MG1655 / ATCC 47076.
  9. "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-9, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  10. Cited for: MALONYLATION AT LYS-9.
    Strain: K12.
  11. "Identification of lysine succinylation as a new post-translational modification."
    Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
    Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION AT LYS-9; LYS-72; LYS-115; LYS-231; LYS-251; LYS-319; LYS-326 AND LYS-348.
    Strain: K12.
  12. "Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase."
    Blom N.S., Tetreault S., Coulombe R., Sygusch J.
    Nat. Struct. Biol. 3:856-862(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH ZINC.
  13. "The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold."
    Cooper S.J., Leonard G.A., McSweeney S.M., Thompson A.W., Naismith J.H., Qamar S., Plater A., Berry A., Hunter W.N.
    Structure 4:1303-1315(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ZINC.
  14. "The crystal structure of Escherichia coli class II fructose-1, 6-bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals details of mechanism and specificity."
    Hall D.R., Leonard G.A., Reed C.D., Watt C.I., Berry A., Hunter W.N.
    J. Mol. Biol. 287:383-394(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC AND TRANSITION STATE ANALOG, ACTIVE SITE.
  15. "The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase."
    Hall D.R., Kemp L.E., Leonard G.A., Marshall K., Berry A., Hunter W.N.
    Acta Crystallogr. D 59:611-614(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CADMIUM, METAL BINDING SITES.

Entry informationi

Entry nameiALF_ECOLI
AccessioniPrimary (citable) accession number: P0AB71
Secondary accession number(s): P11604, Q2M9R7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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