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PSEPA:Q7WST1

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Species (Taxon ID) Pseudomonas paucimobilis (Sphingomonas paucimobilis). (13689)
Gene Name(s) desA
Protein Name(s) Syringate O-demethylase
External Links
UniProt Q7WST1
EMBL AB110975
ProteinModelPortal Q7WST1
BioCyc MetaCyc:MONOMER-15114
GO GO:0005737
GO:0004047
GO:0006546
Gene3D 3.30.1360.120
InterPro IPR013977
IPR006222
IPR027266
Pfam PF01571
PF08669

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0070988

demethylation

PMID:15090517[1]

ECO:0000315

P

Figure 7 shows that analysis of desA mutants is essential to the O demethylation activity of syringate.

complete
CACAO 4783

Contributes to

GO:0018487

vanillate O-demethylase (anaerobic) activity

PMID:15743951[2]

ECO:0000315

F

Fig. 6A: While the vanillate conversion rate of the cell extract of DKLM incubated with vanillate was strikingly reduced, DDAM (ligM and desA double mutant) cells no longer showed any such activity. These results indicated that only ligM and desA are involved in vanillate O demethylation.

complete
CACAO 4991

enables

GO:0008168

methyltransferase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0489

F

Seeded From UniProt

complete

involved_in

GO:0032259

methylation

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0489

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Masai, E et al. (2004) A novel tetrahydrofolate-dependent O-demethylase gene is essential for growth of Sphingomonas paucimobilis SYK-6 with syringate. J. Bacteriol. 186 2757-65 PubMed GONUTS page
  2. Abe, T et al. (2005) A tetrahydrofolate-dependent O-demethylase, LigM, is crucial for catabolism of vanillate and syringate in Sphingomonas paucimobilis SYK-6. J. Bacteriol. 187 2030-7 PubMed GONUTS page