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Protein

L-fuculose phosphate aldolase

Gene

fucA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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.UniRule annotation1 Publication

Catalytic activityi

L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde.UniRule annotation1 Publication

Cofactori

Zn2+UniRule annotation3 PublicationsNote: Binds 1 zinc ion per subunit.UniRule annotation3 Publications

pH dependencei

Optimum pH is 7.2.1 Publication

Pathwayi: L-fucose degradation

This protein is involved in step 3 of the subpathway that synthesizes L-lactaldehyde and glycerone phosphate from L-fucose.UniRule annotation1 Publication
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. L-fucose isomerase (fucI)
  2. L-fuculokinase (fucK)
  3. L-fuculose phosphate aldolase (fucA)
This subpathway is part of the pathway L-fucose degradation, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-lactaldehyde and glycerone phosphate from L-fucose, the pathway L-fucose degradation and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei73Proton acceptor1 Publication1
Metal bindingi73ZincUniRule annotation3 Publications1
Metal bindingi92ZincUniRule annotation3 Publications1
Metal bindingi94ZincUniRule annotation3 Publications1
Active sitei113Proton donor1 Publication1
Metal bindingi155ZincUniRule annotation3 Publications1

GO - Molecular functioni

  • aldehyde-lyase activity Source: EcoCyc
  • L-fuculose-phosphate aldolase activity Source: EcoCyc
  • zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • D-arabinose catabolic process Source: EcoCyc
  • 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.
BRENDAi4.1.2.17. 2026.
SABIO-RKP0AB87.
UniPathwayiUPA00563; UER00626.

Names & Taxonomyi

Protein namesi
Recommended name:
L-fuculose phosphate aldolaseUniRule annotation (EC:4.1.2.17UniRule annotation)
Alternative name(s):
L-fuculose-1-phosphate aldolaseUniRule annotation
Gene namesi
Name:fucAUniRule annotation
Synonyms:fucC, prd
Ordered Locus Names:b2800, JW2771
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10348. fucA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001629251 – 215L-fuculose phosphate aldolaseAdd BLAST215

Proteomic databases

PaxDbiP0AB87.
PRIDEiP0AB87.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation4 Publications

Protein-protein interaction databases

BioGridi4259224. 20 interactors.
DIPiDIP-9710N.
IntActiP0AB87. 1 interactor.
STRINGi511145.b2800.

Structurei

Secondary structure

1215
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 19Combined sources17
Helixi24 – 26Combined sources3
Beta strandi29 – 34Combined sources6
Beta strandi37 – 40Combined sources4
Beta strandi42 – 44Combined sources3
Helixi47 – 49Combined sources3
Helixi52 – 54Combined sources3
Beta strandi56 – 58Combined sources3
Helixi74 – 83Combined sources10
Beta strandi89 – 93Combined sources5
Helixi96 – 104Combined sources9
Beta strandi110 – 112Combined sources3
Helixi113 – 118Combined sources6
Beta strandi120 – 123Combined sources4
Beta strandi131 – 133Combined sources3
Helixi134 – 143Combined sources10
Beta strandi144 – 146Combined sources3
Beta strandi148 – 152Combined sources5
Turni153 – 155Combined sources3
Beta strandi156 – 163Combined sources8
Helixi164 – 185Combined sources22
Helixi196 – 205Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AB87.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldolase class II family. AraD/FucA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107W7X. Bacteria.
COG0235. LUCA.
HOGENOMiHOG000218184.
InParanoidiP0AB87.
KOiK01628.
OMAiYATFGTH.
PhylomeDBiP0AB87.

Family and domain databases

Gene3Di3.40.225.10. 1 hit.
HAMAPiMF_00987. FucA. 1 hit.
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

        10         20         30         40         50
MERNKLARQI IDTCLEMTRL GLNQGTAGNV SVRYQDGMLI TPTGIPYEKL
60 70 80 90 100
TESHIVFIDG NGKHEEGKLP SSEWRFHMAA YQSRPDANAV VHNHAVHCTA
110 120 130 140 150
VSILNRSIPA IHYMIAAAGG NSIPCAPYAT FGTRELSEHV ALALKNRKAT
160 170 180 190 200
LLQHHGLIAC EVNLEKALWL AHEVEVLAQL YLTTLAITDP VPVLSDEEIA
210
VVLEKFKTYG LRIEE
Length:215
Mass (Da):23,775
Last modified:November 8, 2005 - v1
Checksum:iBA9897E13ABE4A22
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000440781.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75842; AAC75842; b2800.
BAE76872; BAE76872; BAE76872.
GeneIDi947282.
KEGGiecj:JW2771.
eco:b2800.
PATRICi32121016. VBIEscCol129921_2900.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000440781.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259224. 20 interactors.
DIPiDIP-9710N.
IntActiP0AB87. 1 interactor.
STRINGi511145.b2800.

Proteomic databases

PaxDbiP0AB87.
PRIDEiP0AB87.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75842; AAC75842; b2800.
BAE76872; BAE76872; BAE76872.
GeneIDi947282.
KEGGiecj:JW2771.
eco:b2800.
PATRICi32121016. VBIEscCol129921_2900.

Organism-specific databases

EchoBASEiEB0344.
EcoGeneiEG10348. fucA.

Phylogenomic databases

eggNOGiENOG4107W7X. Bacteria.
COG0235. LUCA.
HOGENOMiHOG000218184.
InParanoidiP0AB87.
KOiK01628.
OMAiYATFGTH.
PhylomeDBiP0AB87.

Enzyme and pathway databases

UniPathwayiUPA00563; UER00626.
BioCyciEcoCyc:FUCPALDOL-MONOMER.
ECOL316407:JW2771-MONOMER.
MetaCyc:FUCPALDOL-MONOMER.
BRENDAi4.1.2.17. 2026.
SABIO-RKP0AB87.

Miscellaneous databases

EvolutionaryTraceiP0AB87.
PROiP0AB87.

Family and domain databases

Gene3Di3.40.225.10. 1 hit.
HAMAPiMF_00987. FucA. 1 hit.
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.
ProtoNetiSearch...

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: November 2, 2016
This is version 89 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

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 one 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.