ID   A0A1E5P3P2_9ACTN        Unreviewed;       181 AA.
AC   A0A1E5P3P2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Cysteine dioxygenase {ECO:0000313|EMBL:OEJ24145.1};
GN   ORFNames=AS594_06265 {ECO:0000313|EMBL:OEJ24145.1};
OS   Streptomyces agglomeratus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=285458 {ECO:0000313|EMBL:OEJ24145.1, ECO:0000313|Proteomes:UP000095759};
RN   [1] {ECO:0000313|EMBL:OEJ24145.1, ECO:0000313|Proteomes:UP000095759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6-3-2 {ECO:0000313|EMBL:OEJ24145.1,
RC   ECO:0000313|Proteomes:UP000095759};
RA   Chen X.;
RT   "Complete genome sequence of Streptomyces agglomeratus strain 6-3-2, a
RT   novel anti-MRSA actinomycete isolated from Wuli of Tebit, China.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cysteine dioxygenase family.
CC       {ECO:0000256|ARBA:ARBA00006622}.
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:OEJ24145.1}.
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DR   EMBL; MEHJ01000001; OEJ24145.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E5P3P2; -.
DR   STRING; 285458.BGM19_30530; -.
DR   Proteomes; UP000095759; 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:OEJ24145.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000095759};
KW   Thioether bond {ECO:0000256|PIRSR:PIRSR610300-50}.
FT   BINDING         88
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT   BINDING         90
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT   BINDING         144
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT   CROSSLNK        94..160
FT                   /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610300-50"
SQ   SEQUENCE   181 AA;  19514 MW;  489CF40BC8FBA2E1 CRC64;
     MAGRTTRRLA TLISHVREVV RRGLPPDPTA YLVGERLAPH LGADDLLTPG QRTSDPRNYR
     QHLLHAEGDG SFSVVALVWL PGQYTPVHDH VAWCTTGVHA GAEHERRYRL VPSGGGSAAR
     LVATGDFVNT LGTVCGFAPP GDIHRVWNAG TDVAVSLHVY GADLSRLGTS VRRTYEPVPA
     D
//