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HELPX:O30511

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Species (Taxon ID) Helicobacter pylori (Campylobacter pylori). (210)
Gene Name(s) fucT (ECO:0000313 with EMBL:AAB81031.1)
Protein Name(s) Alpha1,3-fucosyltransferase (ECO:0000313 with EMBL:AAB81031.1)
External Links
UniProt O30511
EMBL AF008596
PDB 2NZW
2NZX
2NZY
PDBsum 2NZW
2NZX
2NZY
ProteinModelPortal O30511
SMR O30511
CAZy GT10
BRENDA 2.4.1.214
EvolutionaryTrace O30511
GO GO:0016020
GO:0008417
GO:0006486
InterPro IPR016646
IPR001503
PANTHER PTHR11929
Pfam PF00852
PIRSF PIRSF016150

Annotations

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

enables

GO:0017083

4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity

PMID:17251184[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042803

protein homodimerization activity

PMID:16800635[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0017083

4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity

PMID:16800635[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:9261149[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0017083

4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity

PMID:9261149[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0036065

fucosylation

PMID:9261149[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042806

fucose binding

PMID:17251184[1]

ECO:0000353

physical interaction evidence used in manual assertion

CHEBI:64608

F

Seeded From UniProt

complete

involved_in

GO:0036065

fucosylation

PMID:17251184[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0036065

fucosylation

PMID:16800635[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006486

protein glycosylation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001503

P

Seeded From UniProt

complete

enables

GO:0008417

fucosyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001503

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001503

C

Seeded From UniProt

complete

enables

GO:0017083

4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.4.1.152

F

Seeded From UniProt

complete

involved_in

GO:0009103

lipopolysaccharide biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0448

P

Seeded From UniProt

complete

enables

GO:0016757

transferase activity, transferring glycosyl groups

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0328

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472
UniProtKB-SubCell:SL-0162

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 1.2 Sun, HY et al. (2007) Structure and mechanism of Helicobacter pylori fucosyltransferase. A basis for lipopolysaccharide variation and inhibitor design. J. Biol. Chem. 282 9973-82 PubMed GONUTS page
  2. 2.0 2.1 2.2 Lin, SW et al. (2006) Carboxyl terminus of Helicobacter pylori alpha1,3-fucosyltransferase determines the structure and stability. Biochemistry 45 8108-16 PubMed GONUTS page
  3. 3.0 3.1 3.2 Ge, Z et al. (1997) Cloning and heterologous expression of an alpha1,3-fucosyltransferase gene from the gastric pathogen Helicobacter pylori. J. Biol. Chem. 272 21357-63 PubMed GONUTS page