AGRT5:Q7CVB7

Species (Taxon ID)	Agrobacterium tumefaciens (strain C58 / ATCC 33970). (176299)
Gene Name(s)	sodBII (ECO:0000313 with EMBL:AAK88862.2)
Protein Name(s)	Superoxide dismutase (ECO:0000256 with RuleBase:RU000414)
External Links
UniProt	Q7CVB7
EMBL	AE007870
RefSeq	NP_356077.2
ProteinModelPortal	Q7CVB7
STRING	176299.Atu4583
EnsemblBacteria	AAK88862
GeneID	1136457
KEGG	atu:Atu4583
PATRIC	20818589
eggNOG	COG0605
HOGENOM	HOG000013584
KO	K04564
OMA	MGPGESK
OrthoDB	EOG63NMNT
BioCyc	AGRO:ATU4583-MONOMER
Proteomes	UP000000813
GO	GO:0046872 GO:0004784
InterPro	IPR001189 IPR019833 IPR019832 IPR019831
PANTHER	PTHR11404
Pfam	PF02777 PF00081
PIRSF	PIRSF000349
PRINTS	PR01703
SUPFAM	SSF46609 SSF54719
PROSITE	PS00088

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0004784	superoxide dismutase activity	PMID:19054099	ECO:0000315			F		The role of three iron-containing superoxide dismutase (sodB) genes is shown to protect Agrobacterium tumefaciens against singlet oxygen toxicity in both exponential and stationary growth phases. A sodBI mutant was more sensitive to singlet oxygen than both wild-type bacteria and a double sodBII–sodBIII mutant strain. A sodBI–sodBII double mutant had higher sensitivity to singlet oxygen than a single sodBI mutant, although the double mutant was similar to a sodB null mutant (Figure 2). Cells in the stationary phase were shown to be more vulnerable to damage caused by singlet oxygen than cells in the exponential growth phase. Although SOD exerts a protective effect against both super- oxide anions and singlet oxygen, the response of A. tumefaciens to singlet oxygen was different from the response to super- oxide anion. The avirulent phenotype of the SOD null mutant could be due to the inability to cope with superoxide anions and singlet oxygen generated from plant active defense response to microbial invasion.	complete
involved_in	GO:0019430	removal of superoxide radicals	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004784	P		Seeded From UniProt	complete
involved_in	GO:0019430	removal of superoxide radicals	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004784	P		Seeded From UniProt	complete
enables	GO:0004784	superoxide dismutase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001189 InterPro:IPR019831 InterPro:IPR019832 InterPro:IPR019833	F		Seeded From UniProt	complete
involved_in	GO:0006801	superoxide metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001189 InterPro:IPR019831 InterPro:IPR019832 InterPro:IPR019833	P		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001189 InterPro:IPR019831 InterPro:IPR019832 InterPro:IPR019833	F		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001189 InterPro:IPR019831 InterPro:IPR019832 InterPro:IPR019833	P		Seeded From UniProt	complete
enables	GO:0004784	superoxide dismutase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.15.1.1	F		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0560	P		Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
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References

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