Q65G93

PR
Gene name
mutM
Protein name
Formamidopyrimidine-DNA glycosylase
Names
Fapy-DNA glycosylase, DNA-(apurinic or apyrimidinic site) lyase MutM, AP lyase MutM
Species
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46)
KEGG Pathway
bli:BL00393
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)

108-185 (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 Q65G93

Entry ID Method Resolution Chain Position Source
AF-Q65G93-F1 Predicted AlphaFoldDB

No variants for Q65G93

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q65G93

No associated diseases with Q65G93

5 regional properties for Q65G93

Type Name Position InterPro Accession
domain Zinc finger, DNA glycosylase/AP lyase-type 240 - 274 IPR000214
domain Zinc finger, FPG/IleRS-type 247 - 274 IPR010663
domain Formamidopyrimidine-DNA glycosylase, catalytic domain 1 - 118 IPR012319
domain DNA glycosylase/AP lyase, H2TH DNA-binding 134 - 226 IPR015886
binding_site DNA glycosylase/AP lyase, zinc finger domain, DNA-binding site 249 - 273 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 RRTLAGLVRG KTIDAVDVRW TKIIKRPEEP EEFARLLAGQ TIQSIGRRGK
70 80 90 100 110 120
FLLFHLDDCV MVSHLRMEGK YGLHQNDEPL DKHVHVIFRF TDGSELRYRD VRKFGTMHLF
130 140 150 160 170 180
KPGEELTELP LRQLGPEPFS SEFTADYLRE RLKKTNRSVK TALLDQRTVV GLGNIYVDEA
190 200 210 220 230 240
LFRAGIHPEA TANKLTKKQT VLLHKEIIQT LKEAVEAGGS TVRSYINSQG EIGMFQLKLF
250 260 270
VYGRKDEPCK KCGSPIEKTV VGGRGTHFCI KCQKK