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B9L1Z5

- FPG_THERP

UniProt

B9L1Z5 - FPG_THERP

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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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 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 annotation

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Schiff-base intermediate with DNAUniRule annotation
Active sitei3 – 31Proton donorUniRule annotation
Active sitei60 – 601Proton donor; for beta-elimination activityUniRule annotation
Binding sitei94 – 941DNAUniRule annotation
Binding sitei126 – 1261DNAUniRule annotation
Binding sitei167 – 1671DNAUniRule annotation
Active sitei277 – 2771Proton donor; for delta-elimination activityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri252 – 28736FPG-typeUniRule annotationAdd
BLAST

GO - Molecular functioni

  1. damaged DNA binding Source: InterPro
  2. oxidized purine nucleobase lesion DNA N-glycosylase activity Source: UniProtKB-HAMAP
  3. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. base-excision repair Source: InterPro
  2. nucleotide-excision repair Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Lyase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciTROS309801:GI0S-1882-MONOMER.

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
Ordered Locus Names:trd_1895
OrganismiThermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2)
Taxonomic identifieri309801 [NCBI]
Taxonomic lineageiBacteriaChloroflexiThermomicrobialesThermomicrobiaceaeThermomicrobium
ProteomesiUP000000447: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 289288Formamidopyrimidine-DNA glycosylasePRO_1000118903Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi309801.trd_1895.

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.UniRule annotation
Contains 1 FPG-type zinc finger.UniRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri252 – 28736FPG-typeUniRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0266.
HOGENOMiHOG000020884.
KOiK10563.
OMAiQNTLGMN.
OrthoDBiEOG6QP131.

Family and domain databases

HAMAPiMF_00103. Fapy_DNA_glycosyl.
InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR000191. DNA_glycosylase/AP_lyase.
IPR012319. DNA_glycosylase/AP_lyase_cat.
IPR020629. Formamido-pyr_DNA_Glyclase.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PfamiPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
SMARTiSM00898. Fapy_DNA_glyco. 1 hit.
[Graphical view]
SUPFAMiSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
TIGRFAMsiTIGR00577. fpg. 1 hit.
PROSITEiPS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

B9L1Z5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPELPEVETI RRTLAPVLIG ALVIGALRGE HPEDILLDPW PVFARRVRRH
60 70 80 90 100
RIVALERRGK YLAARFEDGD RLVIHLGMTG ELRLSHPATA PGKHCHLALV
110 120 130 140 150
LRSLRPLPPS LVDQRQRFLL RYLDIRRFGR IALLDQAGWE TFTARLGPEP
160 170 180 190 200
LDPTLDPRAL WSRLRERRTA IKAALLDQAL LAGIGNIYAD EALFQARLHP
210 220 230 240 250
ARRCQTLSLD EVERLLVALR TVLSAAIENA GTTIRDYRDG QGRAGSFQSR
260 270 280
LQVYGKPAGT PCPRCGTGLA RIRIAGRSSV FCPRCQPLH
Length:289
Mass (Da):32,371
Last modified:March 24, 2009 - v1
Checksum:iB1D1DF6F74463784
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001275 Genomic DNA. Translation: ACM05457.1.
RefSeqiYP_002523094.1. NC_011959.1.

Genome annotation databases

EnsemblBacteriaiACM05457; ACM05457; trd_1895.
GeneIDi7356411.
KEGGitro:trd_1895.
PATRICi23914950. VBITheRos91376_1816.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001275 Genomic DNA. Translation: ACM05457.1 .
RefSeqi YP_002523094.1. NC_011959.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 309801.trd_1895.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACM05457 ; ACM05457 ; trd_1895 .
GeneIDi 7356411.
KEGGi tro:trd_1895.
PATRICi 23914950. VBITheRos91376_1816.

Phylogenomic databases

eggNOGi COG0266.
HOGENOMi HOG000020884.
KOi K10563.
OMAi QNTLGMN.
OrthoDBi EOG6QP131.

Enzyme and pathway databases

BioCyci TROS309801:GI0S-1882-MONOMER.

Family and domain databases

HAMAPi MF_00103. Fapy_DNA_glycosyl.
InterProi IPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR000191. DNA_glycosylase/AP_lyase.
IPR012319. DNA_glycosylase/AP_lyase_cat.
IPR020629. Formamido-pyr_DNA_Glyclase.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view ]
Pfami PF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view ]
SMARTi SM00898. Fapy_DNA_glyco. 1 hit.
[Graphical view ]
SUPFAMi SSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
TIGRFAMsi TIGR00577. fpg. 1 hit.
PROSITEi PS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequence of the aerobic CO-oxidizing thermophile Thermomicrobium roseum."
    Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A., Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L., Eisen J.A.
    PLoS ONE 4:E4207-E4207(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27502 / DSM 5159 / P-2.

Entry informationi

Entry nameiFPG_THERP
AccessioniPrimary (citable) accession number: B9L1Z5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: November 26, 2014
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3