ID A0A2H3TPG4_FUSOX Unreviewed; 221 AA.
AC A0A2H3TPG4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=BFJ69_g2612 {ECO:0000313|EMBL:RKK83460.1}, FRV6_09263
GN {ECO:0000313|EMBL:SCO85136.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO85136.1, ECO:0000313|Proteomes:UP000219369};
RN [1] {ECO:0000313|EMBL:SCO85136.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|EMBL:SCO85136.1};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000219369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA Guldener U.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RKK83460.1, ECO:0000313|Proteomes:UP000285084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo_A13 {ECO:0000313|EMBL:RKK83460.1,
RC ECO:0000313|Proteomes:UP000285084};
RX PubMed=30202022; DOI=10.1038/s41598-018-30335-7;
RA Armitage A.D., Taylor A., Sobczyk M.K., Baxter L., Greenfield B.P.,
RA Bates H.J., Wilson F., Jackson A.C., Ott S., Harrison R.J., Clarkson J.P.;
RT "Characterisation of pathogen-specific regions and novel effector
RT candidates in Fusarium oxysporum f. sp. cepae.";
RL Sci. Rep. 8:13530-13530(2018).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MRCX01000013; RKK83460.1; -; Genomic_DNA.
DR EMBL; FMJY01000005; SCO85136.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3TPG4; -.
DR VEuPathDB; FungiDB:FOC1_g10005168; -.
DR VEuPathDB; FungiDB:FOC4_g10011585; -.
DR VEuPathDB; FungiDB:FOIG_11844; -.
DR VEuPathDB; FungiDB:FOMG_12156; -.
DR VEuPathDB; FungiDB:FOXG_08236; -.
DR VEuPathDB; FungiDB:FOZG_07021; -.
DR VEuPathDB; FungiDB:HZS61_012644; -.
DR OrthoDB; 314969at2759; -.
DR Proteomes; UP000219369; Unassembled WGS sequence.
DR Proteomes; UP000285084; 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; 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:0000256|RuleBase:RU366010};
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 ECO:0000256|RuleBase:RU366010};
KW Thioether bond {ECO:0000256|PIRSR:PIRSR610300-50}.
FT BINDING 111
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT BINDING 113
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT CROSSLNK 118..183
FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-50"
SQ SEQUENCE 221 AA; 24562 MW; B6FA2DC05FF7ED57 CRC64;
MAIGIFTKPS ALGVSHSTIP NVGPCQQNRF DELVVRLKDA LGPSSGLTSD DVDVDFLQQL
MEGYDGSDNM WKPYAFGDRS RGYTRNLVDE GNGKSNLLVL VWSPGKGSPI HDHGNAHCLM
KILKGNLTET RYAFPNEDEE QKPMKIIGER TYKENSVAYM ADELGLHRVS NRGSDFAVSL
HLYTPPNVAK KGCHIFDEKT GRKSHVPGCH YYSAYGRLLK E
//
