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STRSU:A0A142UME2

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

public

GO:0008927

mannonate dehydratase activity

PMID:19617363

ECO:0000315

F

Based on fig. 1 (mass spec), two dominant peaks were found after incubation with mannonate dehydratase(ManD). The first peak corresponds to remaining substrate(D-mannonate), whereas the second peak is consistent with formation of the expected protonated dehydration product, 2-KDG (IDA inferred)

Based on table 2, wild type ManD show high affinity to the substrate but the mutant protein Y325F was catalytically inactive while the activity of H311A was only 2.4% that of the native enzyme. The results of site-directed mutagenesis confirmed the functional of these residues in the dehydration reaction (IMP inferred)

complete
CACAO 4480

protected

enables

GO:0008927

mannonate dehydratase activity

PMID:19617363

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

protected

involved_in

GO:0006064

glucuronate catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004628

P

Seeded From UniProt

complete

protected

enables

GO:0008927

mannonate dehydratase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004628

F

Seeded From UniProt

complete

protected

enables

GO:0008927

mannonate dehydratase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.2.1.8

F

Seeded From UniProt

complete

protected

enables

GO:0016829

lyase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

protected

enables

GO:0008927

mannonate dehydratase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000034424

F

Seeded From UniProt

complete




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