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P0AB87

- FUCA_ECOLI

UniProt

P0AB87 - FUCA_ECOLI

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Protein
L-fuculose phosphate aldolase
Gene
fucA, fucC, prd, b2800, JW2771
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the cleavage of L-fuculose 1-phosphate to glycerone phosphate and L-lactaldehyde.1 Publication

Catalytic activityi

L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde.1 Publication

Cofactori

Binds 1 zinc ion per subunit.3 Publications

pH dependencei

Optimum pH is 7.2.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei73 – 731Proton acceptor Inferred
Metal bindingi73 – 731Zinc
Metal bindingi92 – 921Zinc
Metal bindingi94 – 941Zinc
Active sitei113 – 1131Proton donor Inferred
Metal bindingi155 – 1551Zinc

GO - Molecular functioni

  1. L-fuculose-phosphate aldolase activity Source: EcoCyc
  2. aldehyde-lyase activity Source: EcoCyc
  3. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. D-arabinose catabolic process Source: EcoCyc
  2. L-fucose catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism, Fucose metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:FUCPALDOL-MONOMER.
ECOL316407:JW2771-MONOMER.
MetaCyc:FUCPALDOL-MONOMER.
SABIO-RKiP0AB87.
UniPathwayiUPA00563; UER00626.

Names & Taxonomyi

Protein namesi
Recommended name:
L-fuculose phosphate aldolase (EC:4.1.2.17)
Alternative name(s):
L-fuculose-1-phosphate aldolase
Gene namesi
Name:fucA
Synonyms:fucC, prd
Ordered Locus Names:b2800, JW2771
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10348. fucA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215L-fuculose phosphate aldolaseUniRule annotation
PRO_0000162925Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriP0AB87.

Interactioni

Subunit structurei

Homotetramer.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
yneKP761501EBI-1130362,EBI-1128384

Protein-protein interaction databases

DIPiDIP-9710N.
IntActiP0AB87. 1 interaction.
STRINGi511145.b2800.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1917
Helixi24 – 263
Beta strandi29 – 346
Beta strandi37 – 404
Beta strandi42 – 443
Helixi47 – 493
Helixi52 – 543
Beta strandi56 – 583
Helixi74 – 8310
Beta strandi89 – 935
Helixi96 – 1049
Beta strandi110 – 1123
Helixi113 – 1186
Beta strandi120 – 1234
Beta strandi131 – 1333
Helixi134 – 14310
Beta strandi144 – 1463
Beta strandi148 – 1525
Turni153 – 1553
Beta strandi156 – 1638
Helixi164 – 18522
Helixi196 – 20510

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DZUX-ray2.09P1-215[»]
1DZVX-ray1.86P1-215[»]
1DZWX-ray2.17P1-215[»]
1DZXX-ray2.18P1-215[»]
1DZYX-ray2.44P1-213[»]
1DZZX-ray1.92P1-215[»]
1E46X-ray2.55P1-215[»]
1E47X-ray2.15P1-215[»]
1E48X-ray1.97P1-215[»]
1E49X-ray2.53P1-215[»]
1E4AX-ray2.15P1-215[»]
1E4BX-ray1.84P1-215[»]
1E4CX-ray1.66P1-215[»]
1FUAX-ray1.92A1-215[»]
2FUAX-ray2.00A1-215[»]
3FUAX-ray2.67A1-215[»]
4FUAX-ray2.43A1-215[»]
ProteinModelPortaliP0AB87.
SMRiP0AB87. Positions 1-206.

Miscellaneous databases

EvolutionaryTraceiP0AB87.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0235.
HOGENOMiHOG000218184.
KOiK01628.
OMAiYATFGTH.
OrthoDBiEOG6HQSSQ.
PhylomeDBiP0AB87.

Family and domain databases

Gene3Di3.40.225.10. 1 hit.
HAMAPiMF_00987. FucA.
InterProiIPR001303. Aldolase_II/adducin_N.
IPR004782. FucA.
[Graphical view]
PfamiPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTiSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMiSSF53639. SSF53639. 1 hit.
TIGRFAMsiTIGR01086. fucA. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AB87-1 [UniParc]FASTAAdd to Basket

« Hide

MERNKLARQI IDTCLEMTRL GLNQGTAGNV SVRYQDGMLI TPTGIPYEKL    50
TESHIVFIDG NGKHEEGKLP SSEWRFHMAA YQSRPDANAV VHNHAVHCTA 100
VSILNRSIPA IHYMIAAAGG NSIPCAPYAT FGTRELSEHV ALALKNRKAT 150
LLQHHGLIAC EVNLEKALWL AHEVEVLAQL YLTTLAITDP VPVLSDEEIA 200
VVLEKFKTYG LRIEE 215
Length:215
Mass (Da):23,775
Last modified:November 8, 2005 - v1
Checksum:iBA9897E13ABE4A22
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31059 Genomic DNA. Translation: AAA23823.1.
X15025 Genomic DNA. Translation: CAA33125.1.
U29581 Genomic DNA. Translation: AAB40450.1.
U00096 Genomic DNA. Translation: AAC75842.1.
AP009048 Genomic DNA. Translation: BAE76872.1.
M27177 Genomic DNA. No translation available.
PIRiB33495. ADECFP.
RefSeqiNP_417280.1. NC_000913.3.
YP_491008.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75842; AAC75842; b2800.
BAE76872; BAE76872; BAE76872.
GeneIDi12930230.
947282.
KEGGiecj:Y75_p2737.
eco:b2800.
PATRICi32121016. VBIEscCol129921_2900.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31059 Genomic DNA. Translation: AAA23823.1 .
X15025 Genomic DNA. Translation: CAA33125.1 .
U29581 Genomic DNA. Translation: AAB40450.1 .
U00096 Genomic DNA. Translation: AAC75842.1 .
AP009048 Genomic DNA. Translation: BAE76872.1 .
M27177 Genomic DNA. No translation available.
PIRi B33495. ADECFP.
RefSeqi NP_417280.1. NC_000913.3.
YP_491008.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DZU X-ray 2.09 P 1-215 [» ]
1DZV X-ray 1.86 P 1-215 [» ]
1DZW X-ray 2.17 P 1-215 [» ]
1DZX X-ray 2.18 P 1-215 [» ]
1DZY X-ray 2.44 P 1-213 [» ]
1DZZ X-ray 1.92 P 1-215 [» ]
1E46 X-ray 2.55 P 1-215 [» ]
1E47 X-ray 2.15 P 1-215 [» ]
1E48 X-ray 1.97 P 1-215 [» ]
1E49 X-ray 2.53 P 1-215 [» ]
1E4A X-ray 2.15 P 1-215 [» ]
1E4B X-ray 1.84 P 1-215 [» ]
1E4C X-ray 1.66 P 1-215 [» ]
1FUA X-ray 1.92 A 1-215 [» ]
2FUA X-ray 2.00 A 1-215 [» ]
3FUA X-ray 2.67 A 1-215 [» ]
4FUA X-ray 2.43 A 1-215 [» ]
ProteinModelPortali P0AB87.
SMRi P0AB87. Positions 1-206.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-9710N.
IntActi P0AB87. 1 interaction.
STRINGi 511145.b2800.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75842 ; AAC75842 ; b2800 .
BAE76872 ; BAE76872 ; BAE76872 .
GeneIDi 12930230.
947282.
KEGGi ecj:Y75_p2737.
eco:b2800.
PATRICi 32121016. VBIEscCol129921_2900.

Organism-specific databases

EchoBASEi EB0344.
EcoGenei EG10348. fucA.

Phylogenomic databases

eggNOGi COG0235.
HOGENOMi HOG000218184.
KOi K01628.
OMAi YATFGTH.
OrthoDBi EOG6HQSSQ.
PhylomeDBi P0AB87.

Enzyme and pathway databases

UniPathwayi UPA00563 ; UER00626 .
BioCyci EcoCyc:FUCPALDOL-MONOMER.
ECOL316407:JW2771-MONOMER.
MetaCyc:FUCPALDOL-MONOMER.
SABIO-RKi P0AB87.

Miscellaneous databases

EvolutionaryTracei P0AB87.
PROi P0AB87.

Gene expression databases

Genevestigatori P0AB87.

Family and domain databases

Gene3Di 3.40.225.10. 1 hit.
HAMAPi MF_00987. FucA.
InterProi IPR001303. Aldolase_II/adducin_N.
IPR004782. FucA.
[Graphical view ]
Pfami PF00596. Aldolase_II. 1 hit.
[Graphical view ]
SMARTi SM01007. Aldolase_II. 1 hit.
[Graphical view ]
SUPFAMi SSF53639. SSF53639. 1 hit.
TIGRFAMsi TIGR01086. fucA. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation."
    Lu Z., Lin E.C.C.
    Nucleic Acids Res. 17:4883-4884(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Constitutive activation of the fucAO operon and silencing of the divergently transcribed fucPIK operon by an IS5 element in Escherichia coli mutants selected for growth on L-1,2-propanediol."
    Chen Y.M., Lu Z., Lin E.C.C.
    J. Bacteriol. 171:6097-6105(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  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. "Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae."
    Conway T., Ingram L.O.
    J. Bacteriol. 171:3754-3759(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-215.
    Strain: K12.
  6. "The metabolism of L-fucose. II. The enzymatic cleavage of L-fuculose 1-phosphate."
    Ghalambor M.A., Heath E.C.
    J. Biol. Chem. 237:2427-2433(1962) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY.
    Strain: O111:B4.
  7. "The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli."
    Dreyer M.K., Schulz G.E.
    J. Mol. Biol. 231:549-553(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS), COFACTOR, SUBUNIT.
  8. "Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure."
    Dreyer M.K., Schulz G.E.
    J. Mol. Biol. 259:458-466(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) IN COMPLEX WITH ZINC, CATALYTIC MECHANISM, COFACTOR, SUBUNIT, ACTIVE SITES.
  9. "Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli."
    Dreyer M.K., Schulz G.E.
    Acta Crystallogr. D 52:1082-1091(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) IN COMPLEX WITH ZINC, COFACTOR, SUBUNIT.
  10. "Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis."
    Joerger A.C., Gosse C., Fessner W.-D., Schulz G.E.
    Biochemistry 39:6033-6041(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH ZINC, MUTAGENESIS.
  11. "Structures of L-fuculose-1-phosphate aldolase mutants outlining motions during catalysis."
    Joerger A.C., Mueller-Dieckmann C., Schulz G.E.
    J. Mol. Biol. 303:531-543(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF MUTANTS.

Entry informationi

Entry nameiFUCA_ECOLI
AccessioniPrimary (citable) accession number: P0AB87
Secondary accession number(s): P11550, Q2MA34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: May 14, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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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