B5XTG8

PR
Gene name
mutM
Protein name
Formamidopyrimidine-DNA glycosylase
Names
Fapy-DNA glycosylase, DNA-(apurinic or apyrimidinic site) lyase MutM, AP lyase MutM
Species
Klebsiella pneumoniae (strain 342)
KEGG Pathway
kpe:KPK_0119
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)

106-175 (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 B5XTG8

Entry ID Method Resolution Chain Position Source
AF-B5XTG8-F1 Predicted AlphaFoldDB

No variants for B5XTG8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B5XTG8

No associated diseases with B5XTG8

5 regional properties for B5XTG8

Type Name Position InterPro Accession
domain DNA mismatch repair protein MutS, C-terminal 611 - 801 IPR000432
domain DNA mismatch repair protein MutS-like, N-terminal 13 - 124 IPR007695
domain DNA mismatch repair protein MutS, core 274 - 595 IPR007696
domain DNA mismatch repair protein MutS, connector domain 133 - 257 IPR007860
domain DNA mismatch repair protein MutS, clamp 432 - 521 IPR007861

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
MPELPEVETS RRGIEPHLVG VTILHAIVRN GRLRWPVSEE IYRLSDVPVL SVRRRAKYLL
70 80 90 100 110 120
LELPDGWIIV HLGMSGSLRI LSEELPAEKH DHVDLVMSNG KVLRYTDPRR FGAWLWTKTL
130 140 150 160 170 180
EDHPVLAHLG PEPLSDEFNA DYLQQKCAKK KTAIKPWLMD NKLVVGVGNI YASESLFSAG
190 200 210 220 230 240
IHPDRLASSL SREECEQLVK VIKLVLLRSI EQGGTTLKDF LQSDGKPGYF AQELQVYGRK
250 260
GEPCRICGTP VVGTKHAQRA TFYCRQCQK