ID C9YZI0_STRSW Unreviewed; 165 AA.
AC C9YZI0;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Putative cysteine dioxygenase {ECO:0000313|EMBL:CBG72537.1};
GN Name=cdo1 {ECO:0000313|EMBL:CBG72537.1};
GN OrderedLocusNames=SCAB_55071 {ECO:0000313|EMBL:CBG72537.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG72537.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG72537.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG72537.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family.
CC {ECO:0000256|ARBA:ARBA00006622}.
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DR EMBL; FN554889; CBG72537.1; -; Genomic_DNA.
DR RefSeq; WP_013003114.1; NC_013929.1.
DR AlphaFoldDB; C9YZI0; -.
DR STRING; 680198.SCAB_55071; -.
DR GeneID; 24313837; -.
DR KEGG; scb:SCAB_55071; -.
DR eggNOG; COG1917; Bacteria.
DR HOGENOM; CLU_102185_2_0_11; -.
DR Proteomes; UP000001444; Chromosome.
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 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:CBG72537.1};
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:UP000001444}.
FT BINDING 85
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT BINDING 87
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT BINDING 126
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
SQ SEQUENCE 165 AA; 17819 MW; 3D92ED417E8B0787 CRC64;
MNSDSDLQIA GDLLEVPHLL QAPRQHPVTV AEFAGLARSL ADDRSRWEHL VEYDATTRWY
HRLLTGPGYE VWLLSWVPGQ GTGLHGHGGS SGVLTVLDGT LTERTDRGTR VLGAGAQRVF
APGYAHEVVN DALEPAVSLH VYYPGLTEMP MHATACAAQE PAVTA
//
