A6VKA1

PR
Gene name
mutM
Protein name
Formamidopyrimidine-DNA glycosylase
Names
Fapy-DNA glycosylase, DNA-(apurinic or apyrimidinic site) lyase MutM, AP lyase MutM
Species
Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z)
KEGG Pathway
asu:Asuc_0016
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)

105-229 (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 A6VKA1

Entry ID Method Resolution Chain Position Source
AF-A6VKA1-F1 Predicted AlphaFoldDB

No variants for A6VKA1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A6VKA1

No associated diseases with A6VKA1

4 regional properties for A6VKA1

Type Name Position InterPro Accession
domain Zinc finger, DNA glycosylase/AP lyase-type 235 - 269 IPR000214
domain Zinc finger, FPG/IleRS-type 243 - 269 IPR010663
domain Formamidopyrimidine-DNA glycosylase, catalytic domain 1 - 115 IPR012319
domain DNA glycosylase/AP lyase, H2TH DNA-binding 129 - 221 IPR015886

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
MPELPEVETA KNGITPYLDG FYIEKIIVRQ PKLRWEVSPE LSQISHQKVT ALSRRAKYLI
70 80 90 100 110 120
IHTAQGYIIG HLGMSGAVRI VSPDSPVNKH DHLDIVMNNG KIMRYNDPRR FGAWFWTENL
130 140 150 160 170 180
DEFPLFAKLG PEPLSGEFNS DYLFKKSRKK PTAVKSFIMN NAVVVGIGNI YANEVLFQCG
190 200 210 220 230 240
LHPEKPAGKI TKTQAALLTE TIKKELTRAI AQGGTTLKDF LQPDGKPGYF VQELQIYGKK
250 260
GCPCPKCGQK IESFTVGQRN SYVCLHCQKK