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AGRT5:META
Contents
Species (Taxon ID) | Agrobacterium tumefaciens (strain C58 / ATCC 33970). (176299) | |
Gene Name(s) | metA (ECO:0000255 with HAMAP-Rule:MF_00295) | |
Protein Name(s) | Homoserine O-succinyltransferase (ECO:0000255 with HAMAP-Rule:MF_00295)
Homoserine O-transsuccinylase (ECO:0000255 with HAMAP-Rule:MF_00295) HTS (ECO:0000255 with HAMAP-Rule:MF_00295) | |
External Links | ||
UniProt | Q7CWE8 | |
EMBL | AE007869 | |
RefSeq | NP_355651.2 | |
ProteinModelPortal | Q7CWE8 | |
SMR | Q7CWE8 | |
STRING | 176299.Atu2718 | |
DNASU | 1134756 | |
EnsemblBacteria | AAK88436 | |
GeneID | 1134756 | |
KEGG | atu:Atu2718 | |
PATRIC | 20815227 | |
eggNOG | COG1897 | |
HOGENOM | HOG000115049 | |
KO | K00651 | |
OMA | WRSHRNL | |
OrthoDB | EOG61P6ST | |
BioCyc | AGRO:ATU2718-MONOMER MetaCyc:MONOMER-17841 | |
UniPathway | UPA00051 | |
Proteomes | UP000000813 | |
GO | GO:0005737 GO:0008899 GO:0019281 | |
Gene3D | 3.40.50.880 | |
HAMAP | MF_00295 | |
InterPro | IPR029062 IPR005697 | |
PANTHER | PTHR20919 | |
Pfam | PF04204 | |
PIRSF | PIRSF000450 | |
ProDom | PD037892 | |
SUPFAM | SSF52317 | |
TIGRFAMs | TIGR01001 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
Contributes to |
GO:0006508 |
proteolysis |
ECO:0000269 |
P |
The protein is a proteolysis substrate and has high degradation at high temperatures. In Figure 5 it was determined whether or not the metA gene of A. tumefaciens is induced at elevated temperatures. It was found that that there was no induction in the absence of the heat shock transcriptional activator. |
complete | ||||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0008899 |
homoserine O-succinyltransferase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0019281 |
L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004414 |
homoserine O-acetyltransferase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0008899 |
homoserine O-succinyltransferase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000083172 |
F |
Seeded From UniProt |
complete | ||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000083172 |
C |
Seeded From UniProt |
complete | ||
involved_in |
GO:0009086 |
methionine biosynthetic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000083172 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0008652 |
cellular amino acid biosynthetic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0009086 |
methionine biosynthetic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0016740 |
transferase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0016746 |
transferase activity, transferring acyl groups |
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.
- ↑ Rotem, O et al. (2013) Methionine biosynthesis in Agrobacterium tumefaciens: study of the first enzyme. Res. Microbiol. 164 12-6 PubMed GONUTS page