L-fuculose phosphate aldolase - Escherichia coli (strain K12)

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P0AB87 (FUCA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
L-fuculose phosphate aldolase
EC=4.1.2.17

Alternative name(s):
L-fuculose-1-phosphate aldolase

Gene names

Name:	fucA
Synonyms:	fucC, prd
Ordered Locus Names:	b2800, JW2771

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde.
Cofactor	Binds 1 zinc ion per subunit.
Pathway	Carbohydrate degradation; L-fucose degradation; L-lactaldehyde and glycerone phosphate from L-fucose: step 3/3.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the aldolase class II family. AraD/FucA subfamily.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Fucose metabolism
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	D-arabinose catabolic process Inferred from mutant phenotype. Source: EcoCyc L-fucose catabolic process Inferred from mutant phenotype. Source: EcoCyc
Molecular function	L-fuculose-phosphate aldolase activity Inferred from direct assay Ref.9. Source: EcoCyc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
yneK	P76150	1	EBI-1130362,EBI-1128384

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 215

215

L-fuculose phosphate aldolase

PRO_0000162925

Sites

Active site

Proton acceptor Probable

Active site

113

Proton donor Probable

Metal binding

Zinc

Metal binding

Zinc

Metal binding

Zinc

Metal binding

155

Zinc

Secondary structure

215

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AB87 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: BA9897E13ABE4A22
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FASTA

215

23,775

        10         20         30         40         50         60 
MERNKLARQI IDTCLEMTRL GLNQGTAGNV SVRYQDGMLI TPTGIPYEKL TESHIVFIDG 

        70         80         90        100        110        120 
NGKHEEGKLP SSEWRFHMAA YQSRPDANAV VHNHAVHCTA VSILNRSIPA IHYMIAAAGG 

       130        140        150        160        170        180 
NSIPCAPYAT FGTRELSEHV ALALKNRKAT LLQHHGLIAC EVNLEKALWL AHEVEVLAQL 

       190        200        210 
YLTTLAITDP VPVLSDEEIA VVLEKFKTYG LRIEE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2664711] [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: 2553671] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[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]	"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: 2661535] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-215. Strain: K12.
[6]	"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: 8515438] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS).
[7]	"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: 8676381] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), CATALYTIC MECHANISM, ACTIVE SITES.
[8]	"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: 15299567] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[9]	"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: 10821675] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS), MUTAGENESIS.
[10]	"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: 11054289] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF MUTANTS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

ADECFP. B33495.

RefSeq

NP_417280.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0AB87.

SMR

P0AB87. Positions 1-206.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AB87. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004937; EBESCP00000004937; EBESCG00000004028.
EBESCT00000016453; EBESCP00000015744; EBESCG00000015513.

GeneID

947282.

GenomeReviews

Gene locus JW2771 in contig AP009048_GR.
Gene locus b2800 in contig U00096_GR.

KEGG

ecj:JW2771.
eco:b2800.

PATRIC

32121016. VBIEscCol129921_2900.

Organism-specific databases

EchoBASE

EB0344.

EcoGene

EG10348. fucA.

Phylogenomic databases

eggNOG

COG0235.

GeneTree

EBGT00050000009318.

HOGENOM

HBG541069.

OMA

AVYEARP.

PhylomeDB

P0AB87.

ProtClustDB

PRK08087.

Enzyme and pathway databases

BioCyc

EcoCyc:FUCPALDOL-MONOMER.
MetaCyc:FUCPALDOL-MONOMER.

Gene expression databases

Genevestigator

P0AB87.

Family and domain databases

InterPro

IPR001303. Aldolase_II/adducin_N.
IPR004782. FucA.
[Graphical view]

Gene3D

G3DSA:3.40.225.10. Aldolase_II/adducin_N. 1 hit.

K01628.

Pfam

PF00596. Aldolase_II. 1 hit.
[Graphical view]

SMART

SM01007. Aldolase_II. 1 hit.
[Graphical view]

SUPFAM

SSF53639. Aldolase_II_N. 1 hit.

TIGRFAMs

TIGR01086. FucA. 1 hit.

ProtoNet

Search...

Entry information

Entry name

FUCA_ECOLI

Accession

Primary (citable) accession number: P0AB87
Secondary accession number(s): P11550, Q2MA34

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents