ID   A0A0J1CMY2_9BURK        Unreviewed;       180 AA.
AC   A0A0J1CMY2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Cysteine dioxygenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=EOS_32690 {ECO:0000313|EMBL:KLU22070.1};
OS   Caballeronia mineralivorans PML1(12).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU22070.1, ECO:0000313|Proteomes:UP000035963};
RN   [1] {ECO:0000313|EMBL:KLU22070.1, ECO:0000313|Proteomes:UP000035963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX   PubMed=26205858;
RA   Uroz S., Oger P.;
RT   "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT   Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT   Ability.";
RL   Genome Announc. 3:e00798-15(2015).
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:KLU22070.1}.
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DR   EMBL; AEJF01000190; KLU22070.1; -; Genomic_DNA.
DR   RefSeq; WP_047896353.1; NZ_AEJF01000190.1.
DR   AlphaFoldDB; A0A0J1CMY2; -.
DR   PATRIC; fig|908627.4.peg.7302; -.
DR   OrthoDB; 7059163at2; -.
DR   Proteomes; UP000035963; 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};
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         90
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT   BINDING         92
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT   BINDING         143
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT   CROSSLNK        96..161
FT                   /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610300-50"
SQ   SEQUENCE   180 AA;  18660 MW;  827BDEF14C2A5596 CRC64;
     MTLALDPKSP LALLSQTLDQ ACCLDPSSAG FALGVRAALG GLSRGTGLLS DAQRESGLDC
     YRRHLLVADP LGRYAVAALV WQAGQASPVH GHHTWCAYTV IEGTLSETLF AWDADAHRAV
     ATRRHERACG AVSFVGPGRG AIHQLGNASA TGQTAVSIHV YGVPGAQIST HVNDLVAVAA
//