O66602

PR
Gene name
sodC2 (aq_238)
Protein name
Superoxide dismutase [Cu-Zn] 2
Names
Species
Aquifex aeolicus (strain VF5)
KEGG Pathway
aae:aq_238
EC number
1.15.1.1: Acting on superoxide as acceptor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

67-137 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for O66602

Entry ID Method Resolution Chain Position Source
AF-O66602-F1 Predicted AlphaFoldDB

No variants for O66602

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O66602

No associated diseases with O66602

2 regional properties for O66602

Type Name Position InterPro Accession
domain Superoxide dismutase, copper/zinc binding domain 24 - 170 IPR001424
binding_site Superoxide dismutase, copper/zinc, binding site 159 - 170 IPR018152

Functions

Description
EC Number 1.15.1.1 Acting on superoxide as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
copper ion binding Binding to a copper (Cu) ion.
superoxide dismutase activity Catalysis of the reaction: 2 superoxide + 2 H+ = O2 + hydrogen peroxide.

1 GO annotations of biological process

Name Definition
removal of superoxide radicals Any process, acting at the cellular level, involved in removing superoxide radicals (O2-) from a cell or organism, e.g. by conversion to dioxygen (O2) and hydrogen peroxide (H2O2).

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKKLSGVLAG SLLLISASFS QDLKAHAELI NTEGEVIGKA ELIETNSGVL IKLNAKGLPP
70 80 90 100 110 120
NAELAFHIHE RGECKPPTFK SAKGHFNPYG KKHGLLNPEG PHAGDMPNIY TDDKGNVRVQ
130 140 150 160 170
VLNPFVTLKK GEKNSLFKEG GTALVIHSGP DDYKSDPAGN AGKRIACGVI R