ID A0A073J5H7_9RHOB Unreviewed; 200 AA.
AC A0A073J5H7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Dioxygenase {ECO:0000313|EMBL:KEJ96956.1};
GN ORFNames=SUH3_09270 {ECO:0000313|EMBL:KEJ96956.1};
OS Pseudosulfitobacter pseudonitzschiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudosulfitobacter.
OX NCBI_TaxID=1402135 {ECO:0000313|EMBL:KEJ96956.1, ECO:0000313|Proteomes:UP000027746};
RN [1] {ECO:0000313|EMBL:KEJ96956.1, ECO:0000313|Proteomes:UP000027746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3 {ECO:0000313|EMBL:KEJ96956.1,
RC ECO:0000313|Proteomes:UP000027746};
RA Lai Q., Hong Z.;
RT "Sulfitobacter sp. H3 (MCCC 1A00686) Genome Sequencing.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEJ96956.1}.
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DR EMBL; JAMD01000002; KEJ96956.1; -; Genomic_DNA.
DR RefSeq; WP_037922454.1; NZ_WKFG01000017.1.
DR AlphaFoldDB; A0A073J5H7; -.
DR GeneID; 68868195; -.
DR OrthoDB; 9796932at2; -.
DR Proteomes; UP000027746; Unassembled WGS sequence.
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:KEJ96956.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000027746}.
FT DOMAIN 99..200
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 67..69
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 106..108
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 117
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 119
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 191..197
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
SQ SEQUENCE 200 AA; 21859 MW; 4BCAA5EE11101FB3 CRC64;
MTKLILRDVE IHKGFLDRTA QGELLDAVRG VVAAAPLFQP DTPYGKPMSV RMSSAGRYGW
FSDRSGYRYA DRHPSGAPWP PVPEAILAIW DQVTGLARRP DCCLINYYGE GARMGLHQDR
DEADFAWPVV SVSLGDPGLF RVGNPTRGGK TESVWLESGD VVVLGGPARL VYHGVDRIKF
GAGSLLPRGG RINLTLRVVD
//