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ECOLI:RHMA
Contents
Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
Gene Name(s) | rhmA (synonyms: yfaU) | |
Protein Name(s) | 2-keto-3-deoxy-L-rhamnonate aldolase
KDR aldolase 2-dehydro-3-deoxyrhamnonate aldolase 2-keto-3-deoxy acid sugar aldolase | |
External Links | ||
UniProt | P76469 | |
EMBL | U00096 AP009048 | |
PIR | C64995 | |
RefSeq | NP_416748.1 YP_490484.1 | |
PDB | 2VWS 2VWT | |
PDBsum | 2VWS 2VWT | |
ProteinModelPortal | P76469 | |
SMR | P76469 | |
DIP | DIP-11953N | |
STRING | 511145.b2245 | |
EnsemblBacteria | AAC75305 BAA16064 | |
GeneID | 12932490 948054 | |
KEGG | ecj:Y75_p2208 eco:b2245 | |
PATRIC | 32119853 | |
EchoBASE | EB3836 | |
EcoGene | EG14083 | |
eggNOG | COG3836 | |
HOGENOM | HOG000179750 | |
InParanoid | P76469 | |
KO | K12660 | |
OMA | IEGAMRT | |
OrthoDB | EOG6NPM5P | |
PhylomeDB | P76469 | |
BioCyc | EcoCyc:G7158-MONOMER ECOL316407:JW2239-MONOMER MetaCyc:G7158-MONOMER | |
EvolutionaryTrace | P76469 | |
PRO | PR:P76469 | |
Proteomes | UP000000318 UP000000625 | |
Genevestigator | P76469 | |
GO | GO:0005737 GO:0016832 GO:0000287 GO:0016151 GO:0006725 | |
Gene3D | 3.20.20.60 | |
HAMAP | MF_01290 | |
InterPro | IPR005000 IPR023593 IPR015813 | |
Pfam | PF03328 | |
SUPFAM | SSF51621 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
enables |
GO:0016832 |
aldehyde-lyase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG14083 |
F |
Seeded From UniProt |
complete | ||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10016 |
C |
Seeded From UniProt |
complete | ||
enables |
GO:0016832 |
aldehyde-lyase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016151 |
nickel cation binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006725 |
cellular aromatic compound metabolic process |
ECO:0000250 |
sequence similarity evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0016832 |
aldehyde-lyase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003824 |
catalytic activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016832 |
aldehyde-lyase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0106099 |
2-keto-3-deoxy-L-rhamnonate aldolase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0000287 |
magnesium ion binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000101691 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0016832 |
aldehyde-lyase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000101691 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0016829 |
lyase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 2.4 Rea, D et al. (2008) Crystal structure and functional assignment of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12. Biochemistry 47 9955-65 PubMed GONUTS page
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