CDOA_BACSU
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 03-AUG-2022, entry version 117.
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; Firmicutes; 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=3.0 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; O32085; -.
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 OMA; QSIGCAM; -.
DR PhylomeDB; O32085; -.
DR BioCyc; BSUB:BSU31140-MON; -.
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 Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR010300; CDO_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR12918; PTHR12918; 1.
DR Pfam; PF05995; CDO_I; 1.
DR SUPFAM; SSF51182; SSF51182; 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
