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| PROSITE documentation PDOC00082 |
Copper/Zinc superoxide dismutase signatures
Description:
Copper/Zinc superoxide dismutase (EC 1.15.1.1) (SODC) [1] is one of the three
forms of an enzyme that catalyzes the dismutation of superoxide radicals. SODC
binds one atom each of zinc and copper. Various forms of SODC are known: a
cytoplasmic form in eukaryotes, an additional chloroplast form in plants, an
extracellular form in some eukaryotes, and a periplasmic form in prokaryotes.
The metal binding sites are conserved in all the known SODC sequences [2].
We derived two signature patterns for this family of enzymes: the first one
contains two histidine residues that bind the copper atom; the second one is
located in the C-terminal section of SODC and contains a cysteine which is
involved in a disulfide bond.
Note:
These patterns will not detect proteins related to SODC, but which have
lost their catalytic activity, such as Vaccinia virus protein A45.
Last update:
April 2006 / Patterns revised.
Technical section:
PROSITE methods (with tools and information) covered by this documentation:
| SOD_CU_ZN_1, PS00087; Copper/Zinc superoxide dismutase signature 1 (PATTERN) |
| Consensus pattern: |
[GA]-[IMFAT]-H-[LIVF]-H-{S}-x-[GP]-[SDG]-x-[STAGDE]
The 2 H's are copper ligands |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
5. |
|
|
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| Matching PDB structures:
1AZV 1B4L 1BZO 1CB4 ... [ALL] |
| SOD_CU_ZN_2, PS00332; Copper/Zinc superoxide dismutase signature 2 (PATTERN) |
| Consensus pattern: |
G-[GNHD]-[SGA]-[GR]-x-R-x-[SGAWRV]-C-x(2)-[IV]
C is involved in a disulfide bond |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
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|
|
| Matching PDB structures:
1AZV 1B4L 1B4T 1BA9 ... [ALL] |
References:
| 1 |
Authors | Bannister J.V., Bannister W.H., Rotilio G. |
| Title | Aspects of the structure, function, and applications of superoxide dismutase. |
| Source | CRC Crit. Rev. Biochem. 22:111-180(1987). |
| PubMed ID | 3315461 |
| 2 |
Authors | Smith M.W., Doolittle R.F. |
| Title | A comparison of evolutionary rates of the two major kinds of superoxide dismutase. |
| Source | J. Mol. Evol. 34:175-184(1992). |
| PubMed ID | 1556751 |
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