Q9A131

PR
Gene name
mutM
Protein name
Formamidopyrimidine-DNA glycosylase
Names
Fapy-DNA glycosylase, DNA-(apurinic or apyrimidinic site) lyase MutM, AP lyase MutM
Species
Streptococcus pyogenes serotype M1
KEGG Pathway
spz:M5005_Spy0408
EC number
3.2.2.23: Hydrolyzing N-glycosyl compounds
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

107-180 (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 Q9A131

Entry ID Method Resolution Chain Position Source
AF-Q9A131-F1 Predicted AlphaFoldDB

No variants for Q9A131

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9A131

No associated diseases with Q9A131

5 regional properties for Q9A131

Type Name Position InterPro Accession
domain Zinc finger, DNA glycosylase/AP lyase-type 237 - 271 IPR000214
domain Zinc finger, FPG/IleRS-type 243 - 271 IPR010663
domain Formamidopyrimidine-DNA glycosylase, catalytic domain 1 - 117 IPR012319
domain DNA glycosylase/AP lyase, H2TH DNA-binding 131 - 223 IPR015886
binding_site DNA glycosylase/AP lyase, zinc finger domain, DNA-binding site 246 - 270 IPR015887

Functions

Description
EC Number 3.2.2.23 Hydrolyzing N-glycosyl compounds
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

4 GO annotations of molecular function

Name Definition
class I DNA-(apurinic or apyrimidinic site) endonuclease activity Catalysis of the cleavage of an AP site 3' of the baseless site by a beta-lyase mechanism, leaving an unsaturated aldehyde, termed a 3'-(4-hydroxy-5-phospho-2-pentenal) residue, and a 5'-phosphate.
damaged DNA binding Binding to damaged DNA.
oxidized purine nucleobase lesion DNA N-glycosylase activity Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
zinc ion binding Binding to a zinc ion (Zn).

1 GO annotations of biological process

Name Definition
base-excision repair In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPELPEVETV RRGLETLVLG QEIVAVTLKV PKMVKTDLET FALTLPGQII QSVGRRGKYL
70 80 90 100 110 120
LIDLGQLVLV SHLRMEGKYL LFPDEVPDNK HFHVFFELKN GSTLVYQDVR KFGTFDLIAK
130 140 150 160 170 180
SQLSAFFAKR KLGPEPKKET FKLKTFEAAL LSSQKPIKPH LLDQTLVAGL GNIYVDEVLW
190 200 210 220 230 240
AAKVHPETAS SRLNKAEIKR LHDETIRILA LGIEKGGSTV RTYRNALGAD GTMQDYLQVY
250 260 270
GQTGKPCPRC GQAIVKLKVG GRGTHICPKC QKKRL