ID A0A163GEY7_DIDRA Unreviewed; 253 AA.
AC A0A163GEY7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Cysteine dioxygenase {ECO:0000256|ARBA:ARBA00013133, ECO:0000256|RuleBase:RU366010};
DE EC=1.13.11.20 {ECO:0000256|ARBA:ARBA00013133, ECO:0000256|RuleBase:RU366010};
GN ORFNames=ST47_g4045 {ECO:0000313|EMBL:KZM24824.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM24824.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM24824.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM24824.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
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|RuleBase:RU366010};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|RuleBase:RU366010};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000256|RuleBase:RU366010};
CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family.
CC {ECO:0000256|ARBA:ARBA00006622, ECO:0000256|RuleBase:RU366010}.
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:KZM24824.1}.
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DR EMBL; JYNV01000152; KZM24824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163GEY7; -.
DR STRING; 5454.A0A163GEY7; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR GO; GO:0017172; F:cysteine dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd10548; cupin_CDO; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
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; 2.
DR SUPFAM; SSF51182; RmlC-like cupins; 2.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU366010};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU366010};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366010};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU366010};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837};
KW Thioether bond {ECO:0000256|PIRSR:PIRSR610300-50}.
FT CROSSLNK 143..212
FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-50"
SQ SEQUENCE 253 AA; 28047 MW; 36D54FAAAC0D3EA7 CRC64;
MPGRTAEPTD RFQALVQALS DKLGPCSGID SDDVDEKELQ QLMEDYISDE SEWEKYSMAQ
PNTAYTRNLV DKGNGKSNLV PTTLLNGGRD LAFDCTMSKG SVLLTDEATM LADHKIDAST
AQETAGKDTT FDISFSLHAN AHCIMKILKG SLTETRYAWP TVDLNNSEDR HMQVISEKTY
QADQVTYMSD KLGLHRISNP DKDNYAVSLH LYTPPNAAVY GCNVFNEANG RSTHMAKCTV
FSEYGSQVCE ARF
//
