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Database: UniProt
Entry: A5EFW9_BRASB
LinkDB: A5EFW9_BRASB
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ID   A5EFW9_BRASB            Unreviewed;       217 AA.
AC   A5EFW9;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=DNA-N1-methyladenine dioxygenase {ECO:0000313|EMBL:ABQ35063.1};
DE            EC=1.14.11.- {ECO:0000313|EMBL:ABQ35063.1};
GN   Name=alkB {ECO:0000313|EMBL:ABQ35063.1};
GN   OrderedLocusNames=BBta_2936 {ECO:0000313|EMBL:ABQ35063.1};
OS   Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=288000 {ECO:0000313|EMBL:ABQ35063.1, ECO:0000313|Proteomes:UP000000246};
RN   [1] {ECO:0000313|EMBL:ABQ35063.1, ECO:0000313|Proteomes:UP000000246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTAi1 / ATCC BAA-1182 {ECO:0000313|Proteomes:UP000000246};
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604574-2};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604574-2};
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DR   EMBL; CP000494; ABQ35063.1; -; Genomic_DNA.
DR   RefSeq; WP_012043084.1; NC_009485.1.
DR   AlphaFoldDB; A5EFW9; -.
DR   STRING; 288000.BBta_2936; -.
DR   KEGG; bbt:BBta_2936; -.
DR   eggNOG; COG3145; Bacteria.
DR   HOGENOM; CLU_039677_1_1_5; -.
DR   OrthoDB; 9796932at2; -.
DR   Proteomes; UP000000246; Chromosome.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR   InterPro; IPR004574; Alkb.
DR   InterPro; IPR027450; AlkB-like.
DR   InterPro; IPR037151; AlkB-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR16557; ALKYLATED DNA REPAIR PROTEIN ALKB-RELATED; 1.
DR   PANTHER; PTHR16557:SF2; NUCLEIC ACID DIOXYGENASE ALKBH1; 1.
DR   Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:ABQ35063.1};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Iron {ECO:0000256|PIRSR:PIRSR604574-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR604574-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABQ35063.1}.
FT   DOMAIN          117..217
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT   BINDING         80..82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT   BINDING         124..126
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT   BINDING         135
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT   BINDING         137
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT   BINDING         191
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT   BINDING         208..214
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
SQ   SEQUENCE   217 AA;  23483 MW;  BFA023B76705A41E CRC64;
     MAADLFDGLE SAGPARQQLA PGAVLLRGFA RSQQAELIAV IEAIAAQAPF RRMMTPGGHQ
     MSVAMTSCGS CGWVTDRTGY RYDALDPESG QPWPAIPPLF RDLAEQAASE AGFADFAPDA
     CLINRYEPGA KMSLHQDRDE RDIGAPIVSV SLGLPATFLF GGLKRTDKTQ RYRLVHGDVV
     VWGGPARLAF HGIAPLADGE HALLGRRRIN LTFRRAR
//
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