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STRSU:A0A142UME2
Contents
Species (Taxon ID) | Streptococcus suis. (1307) | |
Gene Name(s) | uxuA (ECO:0000256 with HAMAP-Rule:MF_00106) | |
Protein Name(s) | Mannonate dehydratase (ECO:0000256 with HAMAP-Rule:MF_00106, ECO:0000256 with SAAS:SAAS00651377)
D-mannonate hydro-lyase (ECO:0000256 with HAMAP-Rule:MF_00106) | |
External Links | ||
UniProt | A0A142UME2 | |
EMBL | CP012911 | |
RefSeq | WP_002938047.1 | |
ProteinModelPortal | A0A142UME2 | |
UniPathway | UPA00246 | |
Proteomes | UP000070276 | |
GO | GO:0008927 GO:0006064 | |
Gene3D | 3.20.20.150 | |
HAMAP | MF_00106 | |
InterPro | IPR004628 IPR013022 | |
Pfam | PF03786 | |
SUPFAM | SSF51658 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0008927 |
mannonate dehydratase activity |
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 | |||||
enables |
GO:0008927 |
mannonate dehydratase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006064 |
glucuronate catabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0008927 |
mannonate dehydratase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0008927 |
mannonate dehydratase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016829 |
lyase activity |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0008927 |
mannonate dehydratase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000034424 |
F |
Seeded From UniProt |
complete | ||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Zhang, Q et al. (2009) Crystal structures of Streptococcus suis mannonate dehydratase (ManD) and its complex with substrate: genetic and biochemical evidence for a catalytic mechanism. J. Bacteriol. 191 5832-7 PubMed GONUTS page