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Database: UniProt
Entry: R0F5U1_9BRAS
LinkDB: R0F5U1_9BRAS
Original site: R0F5U1_9BRAS 
ID   R0F5U1_9BRAS            Unreviewed;       285 AA.
AC   R0F5U1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=cysteine dioxygenase {ECO:0000256|ARBA:ARBA00013133};
DE            EC=1.13.11.20 {ECO:0000256|ARBA:ARBA00013133};
GN   ORFNames=CARUB_v10005430mg {ECO:0000313|EMBL:EOA17162.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA17162.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
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:0000256|ARBA:ARBA00024284};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20442;
CC         Evidence={ECO:0000256|ARBA:ARBA00024284};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- SIMILARITY: Belongs to the cysteine dioxygenase family.
CC       {ECO:0000256|ARBA:ARBA00006622}.
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DR   EMBL; KB870811; EOA17162.1; -; Genomic_DNA.
DR   RefSeq; XP_006284264.1; XM_006284202.1.
DR   AlphaFoldDB; R0F5U1; -.
DR   STRING; 81985.R0F5U1; -.
DR   GeneID; 17880694; -.
DR   KEGG; crb:17880694; -.
DR   eggNOG; KOG4281; Eukaryota.
DR   OrthoDB; 5487415at2759; -.
DR   Proteomes; UP000029121; Unassembled WGS sequence.
DR   GO; GO:0017172; F:cysteine dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070483; P:detection of hypoxia; IEA:UniProt.
DR   CDD; cd20289; cupin_ADO; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR012864; PCO/ADO.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR22966:SF1; PLANT CYSTEINE OXIDASE 2; 1.
DR   PANTHER; PTHR22966; UNCHARACTERIZED; 1.
DR   Pfam; PF07847; PCO_ADO; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029121}.
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   285 AA;  31458 MW;  EC9C99D0AB35D6DF CRC64;
     MGAGTVVSGR VRKDLSRTNP NVNLPVVTKS TSAETRSNSR KKKIQRRSKT TLISPVQKLV
     DTCKKVFANA KSGTVPSLDK IEMLRSVLDE IKPEDVGVSP KMPYFRSKLT GRSPLVTYLH
     IYACHSFSIG IFCLPSSGVI PLHNHPEMTV FSKLLFGTMH IKSYDWVADC PQPSSDTRLA
     KVKVDSDFTA PCDTSILYPA DGGNMHCFTA KTACAVLDVL GPPYSDPAGR HCTYYFDLPF
     SSFSVDGVAI AEEEKEGHEW LKEREEEPED LTVTAMMYSG PTIKE
//
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