mutM

Functionⁱ

Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.UniRule annotation

Catalytic activityⁱ

Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.UniRule annotationSAAS annotation

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.UniRule annotationSAAS annotation

Cofactorⁱ

Zn²⁺UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	2	Schiff-base intermediate with DNAUniRule annotation	1
Active siteⁱ	3	Proton donorUniRule annotation	1
Active siteⁱ	58	Proton donor; for beta-elimination activityUniRule annotation	1
Binding siteⁱ	92	DNAUniRule annotation	1
Binding siteⁱ	111	DNAUniRule annotation	1
Binding siteⁱ	152	DNAUniRule annotation	1
Active siteⁱ	261	Proton donor; for delta-elimination activityUniRule annotation	1

GO - Molecular functionⁱ

class I DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB-EC
class III/IV DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB-EC
damaged DNA binding Source: InterPro
oxidized purine nucleobase lesion DNA N-glycosylase activity Source: UniProtKB-UniRule
zinc ion binding Source: UniProtKB-UniRule

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

base-excision repair Source: InterPro
nucleotide-excision repair Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-bindingUniRule annotationSAAS annotation, GlycosidaseUniRule annotationSAAS annotation, Hydrolase, LyaseUniRule annotationSAAS annotation, Multifunctional enzymeUniRule annotationSAAS annotation
Biological process	DNA damage, DNA repairUniRule annotationSAAS annotation
Ligand	Metal-binding, Zinc

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Formamidopyrimidine-DNA glycosylaseUniRule annotation (EC:3.2.2.23UniRule annotation) Short name: Fapy-DNA glycosylaseUniRule annotation Alternative name(s): DNA-(apurinic or apyrimidinic site) lyase MutMUniRule annotation (EC:4.2.99.18UniRule annotation) Short name: AP lyase MutMUniRule annotation
Gene namesⁱ	Name:mutMUniRule annotation Synonyms:fpgUniRule annotation ORF Names:P303_11215Imported, P303_11670Imported
Organismⁱ	Xylella fastidiosa MUL0034Imported
Taxonomic identifierⁱ	1401256 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella › Xylella fastidiosa
Proteomesⁱ	UP000027136 Componentⁱ: Chromosome

Interactionⁱ

Subunit structureⁱ

Monomer.UniRule annotationSAAS annotation

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	A0A060HD58.
SMRⁱ	A0A060HD58.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	2 – 114	FPG_CATInterPro annotationAdd BLAST		113
Domainⁱ	237 – 271	FPG-typeInterPro annotationAdd BLAST		35

Sequence similaritiesⁱ

Belongs to the FPG family.UniRule annotationSAAS annotation

Keywords - Domainⁱ

Zinc-fingerUniRule annotationSAAS annotation

Phylogenomic databases

KEGG Orthology (KO) More...KOⁱ	K10563.

KOⁱ

K10563.

Family and domain databases

Gene3Dⁱ	3.20.190.10. 1 hit.
HAMAPⁱ	MF_00103. Fapy_DNA_glycosyl. 1 hit.
InterProⁱ	View protein in InterPro IPR015886. DNA_glyclase/AP_lyase_DNA-bd. IPR015887. DNA_glyclase_Znf_dom_DNA_BS. IPR020629. Formamido-pyr_DNA_Glyclase. IPR012319. FPG_cat. IPR035937. MutM-like_N-ter. IPR010979. Ribosomal_S13-like_H2TH. IPR000214. Znf_DNA_glyclase/AP_lyase.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01149. Fapy_DNA_glyco. 1 hit. PF06831. H2TH. 1 hit.
SMARTⁱ	View protein in SMART SM00898. Fapy_DNA_glyco. 1 hit. SM01232. H2TH. 1 hit.
SUPFAMⁱ	SSF46946. SSF46946. 1 hit. SSF81624. SSF81624. 1 hit.
TIGRFAMsⁱ	TIGR00577. fpg. 1 hit.
PROSITEⁱ	View protein in PROSITE PS51068. FPG_CAT. 1 hit. PS01242. ZF_FPG_1. 1 hit. PS51066. ZF_FPG_2. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

A0A060HD58-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MPELPEVETT LRGLLPYLTN QLIYSLTLRR RTLRWDIPSH IESRLPGHRI 
        60         70         80         90        100
TTVCRRAKYL LIDTNAGGSL IIHLGMSGTL RLLAPETPLR PHDHVDIMLN 
       110        120        130        140        150
NRRVLRFNDP RRFGCLLWQE DGQIHPLLQR LGCEPLSDSF NGDYLYQCSR 
       160        170        180        190        200
ARNVSVKTFL MDQRIVVGVG NIYAAESLFR AGISPLCEAD KISLQRYRRL 
       210        220        230        240        250
AEVVKDILLY AINRGGTTLR DFLSPDGRPG YFKQELFVYG RQQQPCKQCG 
       260        270 
SLLRQTTIRQ RTTVWCGHCQ G

Length:271

Mass (Da):31,091

Last modified:September 3, 2014 - v1

Checksum:ⁱ3FF8AFA1617695DF

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CP006740 Genomic DNA. Translation: AIC13255.1. CP006740 Genomic DNA. Translation: AIC13319.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_004085054.1. NZ_CP006740.1.

Genome annotation databases

EnsemblBacteriaⁱ	AIC13255; AIC13255; P303_11215. AIC13319; AIC13319; P303_11670.
GeneIDⁱ	1125693.
KEGGⁱ	xfl:P303_11215. xfl:P303_11670.

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
A0A060HD58	P64154 P64155 B2I676 A0A0C1D145 A0A1S0VA06 Q3RFD1 A0A1R2D5R8	Xylella fastidiosa (strain 9a5c) Xylella fastidiosa (strain Temecula1 / ATCC 700964) Xylella fastidiosa (strain M23) Xylella fastidiosa Xylella fastidiosa 32 Xylella fastidiosa Dixon Xylella fastidiosa subsp. multiplex	271	UniRef100_P64154	Cluster: Formamidopyrimidine-DNA glycosylase	8

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
A0A060HD58	P64154 P64155 B2I676 A0A0C1D145 A0A1S0VA06 Q3RFD1 A0A1R2D5R8 A0A060H1B6 A0A0Q2Q246 A0A1L2AY96 +2	Xylella fastidiosa (strain 9a5c) Xylella fastidiosa (strain Temecula1 / ATCC 700964) Xylella fastidiosa (strain M23) Xylella fastidiosa Xylella fastidiosa 32 Xylella fastidiosa Dixon Xylella fastidiosa subsp. multiplex Xylella fastidiosa subsp. sandyi Ann-1	271	UniRef90_P64154	Cluster: Formamidopyrimidine-DNA glycosylase	13

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
A0A060HD58	P64154 P64155 B2I676 A0A0C1D145 A0A1S0VA06 Q3RFD1 A0A1R2D5R8 A0A060H1B6 A0A0Q2Q246 UPI000765EB8B +3049	Xylella fastidiosa (strain 9a5c) Xylella fastidiosa (strain Temecula1 / ATCC 700964) Xylella fastidiosa (strain M23) Xylella fastidiosa Xylella fastidiosa 32 Xylella fastidiosa Dixon Xylella fastidiosa subsp. multiplex Xylella fastidiosa subsp. sandyi Ann-1 Marinobacter daepoensis Xylophilus sp. Leaf220 And more	271	UniRef50_P64154	Cluster: Formamidopyrimidine-DNA glycosylase	3,060

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CP006740 Genomic DNA. Translation: AIC13255.1. CP006740 Genomic DNA. Translation: AIC13319.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_004085054.1. NZ_CP006740.1.

3D structure databases

ProteinModelPortalⁱ	A0A060HD58.
SMRⁱ	A0A060HD58.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AIC13255; AIC13255; P303_11215. AIC13319; AIC13319; P303_11670.
GeneIDⁱ	1125693.
KEGGⁱ	xfl:P303_11215. xfl:P303_11670.

Phylogenomic databases

KEGG Orthology (KO) More...KOⁱ	K10563.

KOⁱ

K10563.

Family and domain databases

Gene3Dⁱ	3.20.190.10. 1 hit.
HAMAPⁱ	MF_00103. Fapy_DNA_glycosyl. 1 hit.
InterProⁱ	View protein in InterPro IPR015886. DNA_glyclase/AP_lyase_DNA-bd. IPR015887. DNA_glyclase_Znf_dom_DNA_BS. IPR020629. Formamido-pyr_DNA_Glyclase. IPR012319. FPG_cat. IPR035937. MutM-like_N-ter. IPR010979. Ribosomal_S13-like_H2TH. IPR000214. Znf_DNA_glyclase/AP_lyase.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01149. Fapy_DNA_glyco. 1 hit. PF06831. H2TH. 1 hit.
SMARTⁱ	View protein in SMART SM00898. Fapy_DNA_glyco. 1 hit. SM01232. H2TH. 1 hit.
SUPFAMⁱ	SSF46946. SSF46946. 1 hit. SSF81624. SSF81624. 1 hit.
TIGRFAMsⁱ	TIGR00577. fpg. 1 hit.
PROSITEⁱ	View protein in PROSITE PS51068. FPG_CAT. 1 hit. PS01242. ZF_FPG_1. 1 hit. PS51066. ZF_FPG_2. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	A0A060HD58_XYLFS
Accessionⁱ	A0A060HD58Primary (citable) accession number: A0A060HD58
Entry historyⁱ	Integrated into UniProtKB/TrEMBL:	September 3, 2014
	Last sequence update:	September 3, 2014
	Last modified:	March 28, 2018
	This is version 27 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Unreviewed (UniProtKB/TrEMBL)

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteomeImported

UniProtKB - A0A060HD58 (A0A060HD58_XYLFS)

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Formamidopyrimidine-DNA glycosylase

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Functionⁱ

Catalytic activityⁱ

Cofactorⁱ

Sites

GO - Molecular functionⁱ

GO - Biological processⁱ

Keywordsⁱ

Names & Taxonomyⁱ

Interactionⁱ

Subunit structureⁱ

Structureⁱ

3D structure databases

Family & Domainsⁱ

Domains and Repeats

Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

Sequenceⁱ

Sequence databases

Genome annotation databases

Similar proteinsⁱ

Cross-referencesⁱ

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - A0A060HD58 (A0A060HD58_XYLFS)

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Formamidopyrimidine-DNA glycosylase

mutM

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

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3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

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Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ