ID A0A344PIA8_9RHOB Unreviewed; 214 AA.
AC A0A344PIA8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Alpha-ketoglutarate-dependent dioxygenase AlkB {ECO:0000313|EMBL:AXC49113.1};
GN ORFNames=DRW48_04935 {ECO:0000313|EMBL:AXC49113.1};
OS Paracoccus suum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=2259340 {ECO:0000313|EMBL:AXC49113.1, ECO:0000313|Proteomes:UP000252023};
RN [1] {ECO:0000313|Proteomes:UP000252023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2-6 {ECO:0000313|Proteomes:UP000252023};
RA Heo J., Kim S.-J., Kwon S.-W.;
RT "Genome sequencing of Paracoccus sp. SC2-6.";
RL Submitted (JUL-2018) 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};
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DR EMBL; CP030918; AXC49113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A344PIA8; -.
DR KEGG; pars:DRW48_04935; -.
DR OrthoDB; 9796932at2; -.
DR Proteomes; UP000252023; 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:AXC49113.1};
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:UP000252023}.
FT DOMAIN 111..212
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 79..81
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 118..120
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 129
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 131
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
FT BINDING 185
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT BINDING 203..209
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR604574-1"
SQ SEQUENCE 214 AA; 22746 MW; 94EBD13D6593A14B CRC64;
MSFSQILPGQ AAKAALTIRG ASLWPGLLDP DAQAALMADV ARIWAAAPPR QLLTRWNKPL
SVSMSAAGAC GWTSDRRGYR YAPTQDDGNP WPPIPEALLA LWRAVVPEAQ APDSLLVNLY
RGRARMGLHQ DRDEADFGQP VVSVSLGDAA LFRIGGTERG DPTESVWLNS GDVLVLAGSA
RLAFHGIDRI REGSSNLVPG GGRVNLTLRV AGCG
//
