ID   CDOA_BACSU              Reviewed;         161 AA.
AC   O32085;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Cysteine dioxygenase;
DE            Short=CDO;
DE            EC=1.13.11.20;
GN   Name=cdoA; Synonyms=yubC; OrderedLocusNames=BSU31140;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DEVELOPMENTAL STAGE.
RX   PubMed=16855246; DOI=10.1128/jb.00291-06;
RA   Dominy J.E. Jr., Simmons C.R., Karplus P.A., Gehring A.M., Stipanuk M.H.;
RT   "Identification and characterization of bacterial cysteine dioxygenases: a
RT   new route of cysteine degradation for eubacteria.";
RL   J. Bacteriol. 188:5561-5569(2006).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH IRON.
RX   PubMed=25307852; DOI=10.1002/pro.2587;
RA   Driggers C.M., Hartman S.J., Karplus P.A.;
RT   "Structures of Arg- and Gln-type bacterial cysteine dioxygenase homologs.";
RL   Protein Sci. 24:154-161(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteine + O2 = 3-sulfino-L-alanine + H(+);
CC         Xref=Rhea:RHEA:20441, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:61085; EC=1.13.11.20;
CC         Evidence={ECO:0000269|PubMed:16855246};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3 mM for cysteine {ECO:0000269|PubMed:16855246};
CC       pH dependence:
CC         Optimum pH is 6.2. {ECO:0000269|PubMed:16855246};
CC   -!- DEVELOPMENTAL STAGE: Up-regulated upon sporulation.
CC       {ECO:0000269|PubMed:16855246}.
CC   -!- MISCELLANEOUS: Although there are Cys and Trp residues in equivalent
CC       positions with the residues forming a thioether cross-link in the
CC       eukaryotic homologous sequences, no thioether cross-link is formed in
CC       this protein. {ECO:0000269|PubMed:25307852}.
CC   -!- SIMILARITY: Belongs to the cysteine dioxygenase family. {ECO:0000305}.
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DR   EMBL; AL009126; CAB15092.1; -; Genomic_DNA.
DR   PIR; F70006; F70006.
DR   RefSeq; NP_390992.1; NC_000964.3.
DR   RefSeq; WP_003243534.1; NZ_JNCM01000033.1.
DR   PDB; 3EQE; X-ray; 2.82 A; A/B=1-161.
DR   PDB; 4QM8; X-ray; 2.82 A; A/B=1-161.
DR   PDB; 4QM9; X-ray; 2.30 A; A/B=1-161.
DR   PDBsum; 3EQE; -.
DR   PDBsum; 4QM8; -.
DR   PDBsum; 4QM9; -.
DR   AlphaFoldDB; O32085; -.
DR   SMR; O32085; -.
DR   STRING; 224308.BSU31140; -.
DR   PaxDb; 224308-BSU31140; -.
DR   DNASU; 938837; -.
DR   EnsemblBacteria; CAB15092; CAB15092; BSU_31140.
DR   GeneID; 938837; -.
DR   KEGG; bsu:BSU31140; -.
DR   PATRIC; fig|224308.179.peg.3374; -.
DR   eggNOG; COG5553; Bacteria.
DR   InParanoid; O32085; -.
DR   OrthoDB; 7059163at2; -.
DR   PhylomeDB; O32085; -.
DR   BioCyc; BSUB:BSU31140-MONOMER; -.
DR   BRENDA; 1.13.11.20; 658.
DR   SABIO-RK; O32085; -.
DR   EvolutionaryTrace; O32085; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0017172; F:cysteine dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..161
FT                   /note="Cysteine dioxygenase"
FT                   /id="PRO_0000360761"
FT   BINDING         75
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:25307852"
FT   BINDING         77
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:25307852"
FT   BINDING         125
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:25307852"
FT   HELIX           3..11
FT                   /evidence="ECO:0007829|PDB:4QM9"
FT   HELIX           19..26
FT                   /evidence="ECO:0007829|PDB:4QM9"
FT   HELIX           32..36
FT                   /evidence="ECO:0007829|PDB:4QM9"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:4QM9"
FT   STRAND          44..55
FT                   /evidence="ECO:0007829|PDB:4QM9"
FT   STRAND          60..66
FT                   /evidence="ECO:0007829|PDB:4QM9"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:4QM8"
FT   STRAND          81..98
FT                   /evidence="ECO:0007829|PDB:4QM9"
FT   STRAND          100..112
FT                   /evidence="ECO:0007829|PDB:4QM9"
FT   STRAND          116..119
FT                   /evidence="ECO:0007829|PDB:4QM9"
FT   STRAND          124..128
FT                   /evidence="ECO:0007829|PDB:4QM9"
FT   STRAND          131..133
FT                   /evidence="ECO:0007829|PDB:4QM9"
FT   STRAND          135..143
FT                   /evidence="ECO:0007829|PDB:4QM9"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:4QM8"
SQ   SEQUENCE   161 AA;  18127 MW;  9580D43AE8AFE016 CRC64;
     MELYECIQDI FGGLKNPSVK DLATSLKQIP NAAKLSQPYI KEPDQYAYGR NAIYRNNELE
     IIVINIPPNK ETTVHDHGQS IGCAMVLEGK LLNSIYRSTG EHAELSNSYF VHEGECLIST
     KGLIHKMSNP TSERMVSLHV YSPPLEDMTV FEEQKEVLEN S
//