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Q58813 (FUCA_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-fuculose phosphate aldolase

EC=4.1.2.17
Alternative name(s):
L-fuculose-1-phosphate aldolase
Gene names
Name:fucA
Ordered Locus Names:MJ1418
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length181 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible aldol cleavage of L-fuculose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde. The substrate preference order is glyceraldehyde > DL-lactaldehyde, glycolaldehyde > acrolein > formaldehyde, methylglyoxal > acetaldehyde > crotonaldehyde. No activity was observed towards propionaldehyde. Ref.2

Catalytic activity

L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde. Ref.2

Cofactor

Binds 1 zinc ion per subunit Potential.

Pathway

Carbohydrate degradation; L-fucose degradation; L-lactaldehyde and glycerone phosphate from L-fucose: step 3/3.

Cofactor biosynthesis; coenzyme F420 biosynthesis.

Subunit structure

Homotetramer. Ref.2

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

Vmax=570 nmol/min/mg enzyme with glyceraldehyde as substrate (at pH 7.4 and at 70 degrees Celsius) Ref.2

Vmax=501 nmol/min/mg enzyme with DL-lactaldehyde as substrate (at pH 7.4 and at 70 degrees Celsius)

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfucose catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionL-fuculose-phosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 181181L-fuculose phosphate aldolase
PRO_0000162932

Sites

Metal binding681Zinc By similarity
Metal binding871Zinc By similarity
Metal binding891Zinc By similarity
Metal binding1471Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q58813 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E5F3BF13722145B0

FASTA18120,470
        10         20         30         40         50         60 
MDKKQFIKIC RKLYDRKYVV GSGGNVSVKE GDKIYLTPTG SILGFLKEDD IAEMDLDGNV 

        70         80         90        100        110        120 
IKGKPTSEKN LHLMIYRKRN DINAIIHTHS LISTFLSTIN KEIELLTPEG KIFLKKIGYV 

       130        140        150        160        170        180 
DYYEAGSLKL AEETAKRDED VIILKNHGVV CLGKDLIDAY IKVEVLEEQA KLTLLNLLVK 


K 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii."
Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. expand/collapse author list , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]"Identification of lactaldehyde dehydrogenase in Methanocaldococcus jannaschii and its involvement in production of lactate for F420 biosynthesis."
Grochowski L.L., Xu H., White R.H.
J. Bacteriol. 188:2836-2844(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN F420 BIOSYNTHESIS, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB99428.1.
PIRA64477.
RefSeqNP_248422.1. NC_000909.1.

3D structure databases

ProteinModelPortalQ58813.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ1418.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB99428; AAB99428; MJ_1418.
GeneID1452322.
KEGGmja:MJ_1418.

Phylogenomic databases

eggNOGCOG0235.
KOK01628.
OMAPVVWESS.
ProtClustDBCLSK876567.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12176.
UniPathwayUPA00071.
UPA00563; UER00626.

Family and domain databases

Gene3D3.40.225.10. 1 hit.
InterProIPR001303. Aldolase_II/adducin_N.
[Graphical view]
PfamPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMSSF53639. SSF53639. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFUCA_METJA
AccessionPrimary (citable) accession number: Q58813
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names