ID A0A1I5FZB2_9PSEU Unreviewed; 178 AA.
AC A0A1I5FZB2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Cysteine dioxygenase type I {ECO:0000313|EMBL:SFO29078.1};
GN ORFNames=SAMN05421805_11218 {ECO:0000313|EMBL:SFO29078.1};
OS Saccharopolyspora antimicrobica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=455193 {ECO:0000313|EMBL:SFO29078.1, ECO:0000313|Proteomes:UP000199398};
RN [1] {ECO:0000313|EMBL:SFO29078.1, ECO:0000313|Proteomes:UP000199398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 201259 {ECO:0000313|EMBL:SFO29078.1,
RC ECO:0000313|Proteomes:UP000199398};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family.
CC {ECO:0000256|ARBA:ARBA00006622}.
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DR EMBL; FOUP01000012; SFO29078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5FZB2; -.
DR STRING; 455193.SAMN05421805_11218; -.
DR Proteomes; UP000199398; Unassembled WGS sequence.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR CDD; cd10548; cupin_CDO; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR010300; CDO_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR12918; CYSTEINE DIOXYGENASE; 1.
DR PANTHER; PTHR12918:SF1; CYSTEINE DIOXYGENASE TYPE 1; 1.
DR Pfam; PF05995; CDO_I; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:SFO29078.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR610300-51};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR610300-51};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Thioether bond {ECO:0000256|PIRSR:PIRSR610300-50}.
FT BINDING 91
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT BINDING 93
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT BINDING 141
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT CROSSLNK 97..157
FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-50"
SQ SEQUENCE 178 AA; 19357 MW; 1548FE7514238872 CRC64;
MPGKVIRMTT QLIELAGTIR EQVRRGLPAA QTAELVEDAL KPFLTAPDLL SPVQRVGDPD
HYRQHVLHVE PDGSFSIVAL VWLPGQQTPV HDHISWCVTG VHEGVEHEQR YVLREGDLVP
AEQTTNHPGE VCGFAPPGDI HLVRNAGSVK AISIHVYGAD IAVLGSSVRR CYELGATA
//