ID A0A0A0F3K6_9GAMM Unreviewed; 230 AA.
AC A0A0A0F3K6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Fe(II)-dependent oxygenase {ECO:0000313|EMBL:KGM56908.1};
GN ORFNames=N799_01770 {ECO:0000313|EMBL:KGM56908.1};
OS Lysobacter arseniciresistens ZS79.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=913325 {ECO:0000313|EMBL:KGM56908.1, ECO:0000313|Proteomes:UP000029989};
RN [1] {ECO:0000313|EMBL:KGM56908.1, ECO:0000313|Proteomes:UP000029989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS79 {ECO:0000313|EMBL:KGM56908.1,
RC ECO:0000313|Proteomes:UP000029989};
RX PubMed=26516404; DOI=10.1186/s40793-015-0070-5;
RA Liu L., Zhang S., Luo M., Wang G.;
RT "Genomic information of the arsenic-resistant bacterium Lysobacter
RT arseniciresistens type strain ZS79(T) and comparison of Lysobacter draft
RT genomes.";
RL Stand. Genomic Sci. 10:88-88(2015).
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00657};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00657};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961,
CC ECO:0000256|HAMAP-Rule:MF_00657};
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:KGM56908.1}.
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DR EMBL; AVPT01000007; KGM56908.1; -; Genomic_DNA.
DR RefSeq; WP_036209210.1; NZ_AVPT01000007.1.
DR AlphaFoldDB; A0A0A0F3K6; -.
DR STRING; 913325.N799_01770; -.
DR eggNOG; COG3128; Bacteria.
DR OrthoDB; 9812472at2; -.
DR Proteomes; UP000029989; Unassembled WGS sequence.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR Gene3D; 4.10.860.20; Rabenosyn, Rab binding domain; 1.
DR HAMAP; MF_00657; Hydroxyl_YbiX; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR041097; PKHD_C.
DR InterPro; IPR023550; PKHD_hydroxylase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR PANTHER; PTHR41536; PKHD-TYPE HYDROXYLASE YBIX; 1.
DR PANTHER; PTHR41536:SF1; PKHD-TYPE HYDROXYLASE YBIX; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF18331; PKHD_C; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|HAMAP-
KW Rule:MF_00657};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00657};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00657};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00657}; Reference proteome {ECO:0000313|Proteomes:UP000029989};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896, ECO:0000256|HAMAP-Rule:MF_00657}.
FT DOMAIN 78..182
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT BINDING 96
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00657"
FT BINDING 98
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00657"
FT BINDING 163
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00657"
FT BINDING 173
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00657"
SQ SEQUENCE 230 AA; 25200 MW; 995A2EFFAA1D642B CRC64;
MLLHIPGILD DAQLARFRQS LDAAAWTDGR QTVGPQGAQV KRNLQLPEDS PLRQQLGREV
LAALAANPLY FAAALPARTL PPRFNRYEGG GRYGFHVDGA VMAMAVPDGL PPVNLRSDVS
CTLFLCDPDE YDGGELVIHD TYGEHEVKLP AGDLVVYPSS SLHRVAPVTR GARVAAFFWV
QSLVRDDGER RMLFELDQAI QALTASGADG EAVLRLTGVY HNLLRRWAET
//
