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AGRFC:GCI

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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

PMID:24926996[1]

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

PMID:22493433[2]

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

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR018110

P

Seeded From UniProt

complete

enables

GO:0016853

isomerase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR034618

F

Seeded From UniProt

complete

enables

GO:0016853

isomerase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0413

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 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
  2. 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