ID A0A317VDF7_9EURO Unreviewed; 249 AA.
AC A0A317VDF7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=BO70DRAFT_320774 {ECO:0000313|EMBL:PWY72403.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY72403.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY72403.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY72403.1,
RC ECO:0000313|Proteomes:UP000247233};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:PWY72403.1}.
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DR EMBL; MSFL01000026; PWY72403.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317VDF7; -.
DR STRING; 1448321.A0A317VDF7; -.
DR VEuPathDB; FungiDB:BO70DRAFT_320774; -.
DR OrthoDB; 314969at2759; -.
DR Proteomes; UP000247233; 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|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 Reference proteome {ECO:0000313|Proteomes:UP000247233};
KW Thioether bond {ECO:0000256|PIRSR:PIRSR610300-50}.
FT BINDING 99
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT BINDING 189
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT CROSSLNK 106..206
FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-50"
SQ SEQUENCE 249 AA; 28192 MW; 8650206970A2D0F6 CRC64;
MPYIETDSFS ETPGSNGFDK LVRDLRDVLG PSSGLDSDDI DPMDVQRLME QYDSNSEDWI
SLALADPKKN YTRNLIDEGN GKSNLLILVW TPGKRSPIHD HANAHCVMKA RSYPIYTSHS
KKPQVHTDRD PQTKPQNIQI LKGSLQETLY SWPDKDKLSH GHPSPPQVKR QTVYTENQVT
YMSDKLGLHR ISNPDPNEYA VSLHLYTPPN AVTYGFYIYD DDTGKPSHIP SAHVYSVRGK
RTRDNPESA
//
