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AGRFC:GCI
Contents
Species (Taxon ID) | Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacteriumtumefaciens (strain C58)). (176299) | |
Gene Name(s) | gci | |
Protein Name(s) | D-galactarolactone cycloisomerase | |
External Links | ||
UniProt | A9CEQ8 | |
EMBL | AE007870 | |
PIR | AE2942 E98340 | |
RefSeq | NP_357462.1 WP_010972789.1 | |
PDB | 4GGB 4HPN | |
PDBsum | 4GGB 4HPN | |
ProteinModelPortal | A9CEQ8 | |
STRING | 176299.Atu3139 | |
EnsemblBacteria | AAK90247 | |
GeneID | 1134941 | |
KEGG | atu:Atu3139 | |
PATRIC | 20815744 | |
eggNOG | ENOG4105CXK COG4948 | |
HOGENOM | HOG000113756 | |
KO | K18983 | |
OrthoDB | EOG65BDGD | |
BioCyc | AGRO:ATU3139-MONOMER | |
UniPathway | UPA01050 | |
Proteomes | UP000000813 | |
GO | GO:0016853 GO:0046872 GO:0009063 | |
Gene3D | 3.20.20.120 3.30.390.10 | |
InterPro | IPR029065 IPR029017 IPR018110 IPR013342 IPR013341 IPR001354 | |
PANTHER | PTHR13794 | |
Pfam | PF13378 PF02746 | |
SMART | SM00922 | |
SUPFAM | SSF51604 SSF54826 | |
PROSITE | PS00908 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
Contributes to |
GO:0003824 |
catalytic activity |
ECO:0000269 |
F |
A9CG74 has a DxH motif at the end of β-strand 3 similar to the catalytic residues in D-galactonate dehydratases (Figure 1) but does not catalyze the dehydration of D-galactonate; D-galactonate dehydratases do not catalyze the dehydration of m-galactarate or D-galacturonate. An alignment of the sequences in this cluster shows that both the active site catalytic residues and substrate binding residues in the capping domain are conserved (Figure 1). The enzymes in this cluster likely are orthologues based on sequence identity and shared catalytic/ substrate specificity-determining residues. |
complete | ||||
Contributes to |
GO:0009063 |
cellular amino acid catabolic process |
ECO:0000314 |
P |
Different pathways for d-galacturonate catabolism take place. It is active both on d-galactarolactone and d-glucarolactone, but does not work on the corresponding linear hexaric acid forms. These verifications are confirmed through the use of a gel (Fig. 2). Figure 1 shows the reaction scheme of the first steps of the oxidation pathways, which further clarify the function. |
complete | ||||
involved_in |
GO:0009063 |
cellular amino acid catabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0016853 |
isomerase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016853 |
isomerase 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.
- ↑ Groninger-Poe, FP et al. (2014) Evolution of enzymatic activities in the enolase superfamily: galactarate dehydratase III from Agrobacterium tumefaciens C58. Biochemistry 53 4192-203 PubMed GONUTS page
- ↑ Andberg, M et al. (2012) Characterization of a novel Agrobacterium tumefaciens galactarolactone cycloisomerase enzyme for direct conversion of D-galactarolactone to 3-deoxy-2-keto-L-threo-hexarate. J. Biol. Chem. 287 17662-71 PubMed GONUTS page