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Database: UniProt
Entry: A0A1I5FZB2_9PSEU
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Original site: A0A1I5FZB2_9PSEU 
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
//
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