CDO_ARTBC
ID CDO_ARTBC Reviewed; 219 AA.
AC D4AN26;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 2.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Cysteine dioxygenase {ECO:0000303|PubMed:23353986};
DE Short=CDO {ECO:0000303|PubMed:23353986};
DE EC=1.13.11.20 {ECO:0000269|PubMed:21039937};
GN Name=CDO1 {ECO:0000303|PubMed:23353986};
GN ORFNames=ARB_05630 {ECO:0000312|EMBL:EFE35587.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=21039937; DOI=10.1111/j.1439-0507.2010.01948.x;
RA Kasperova A., Kunert J., Horynova M., Weigl E., Sebela M., Lenobel R.,
RA Raska M.;
RT "Isolation of recombinant cysteine dioxygenase protein from Trichophyton
RT mentagrophytes.";
RL Mycoses 54:E456-E462(2011).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23353986; DOI=10.1038/jid.2013.41;
RA Grumbt M., Monod M., Yamada T., Hertweck C., Kunert J., Staib P.;
RT "Keratin degradation by dermatophytes relies on cysteine dioxygenase and a
RT sulfite efflux pump.";
RL J. Invest. Dermatol. 133:1550-1555(2013).
RN [4]
RP INDUCTION, AND POST-TRANSLATIONAL MODIFICATION.
RX PubMed=25040038; DOI=10.1111/myc.12220;
RA Kasperova A., Cahlikova R., Kunert J., Sebela M., Novak Z., Raska M.;
RT "Exposition of dermatophyte Trichophyton mentagrophytes to L-cystine
RT induces expression and activation of cysteine dioxygenase.";
RL Mycoses 57:672-678(2014).
CC -!- FUNCTION: Cysteine dioxygenase involved in sulfite formation from
CC cysteine. Required for keratin degradation and plays an important role
CC in filamentous growth and virulence. {ECO:0000269|PubMed:21039937,
CC ECO:0000269|PubMed:23353986}.
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:21039937};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:Q16878};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250|UniProtKB:Q16878};
CC -!- INDUCTION: Induced by L-cysteine. {ECO:0000269|PubMed:25040038}.
CC -!- PTM: The thioether cross-link between Cys-113 and Tyr-183 plays a
CC structural role through stabilizing the Fe(2+) ion, and prevents the
CC production of highly damaging free hydroxyl radicals by holding the
CC oxygen radical via hydroxyl hydrogen. {ECO:0000250|UniProtKB:Q16878}.
CC -!- DISRUPTION PHENOTYPE: Leads to hypersensitivity to L-cysteine.
CC Abolishes the ability to grow on human hair and nails as substrates.
CC {ECO:0000269|PubMed:23353986}.
CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFE35587.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; ABSU01000003; EFE35587.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003016232.1; XM_003016186.1.
DR AlphaFoldDB; D4AN26; -.
DR SMR; D4AN26; -.
DR STRING; 663331.D4AN26; -.
DR EnsemblFungi; EFE35587; EFE35587; ARB_05630.
DR GeneID; 9524303; -.
DR KEGG; abe:ARB_05630; -.
DR HOGENOM; CLU_079443_4_1_1; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0017172; F:cysteine dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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 Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Thioether bond; Virulence.
FT CHAIN 1..219
FT /note="Cysteine dioxygenase"
FT /id="PRO_0000432123"
FT BINDING 106
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q16878"
FT BINDING 108
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q16878"
FT BINDING 166
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q16878"
FT CROSSLNK 113..183
FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:Q16878"
SQ SEQUENCE 219 AA; 24546 MW; 15968ACFD846F774 CRC64;
MPFIENQTTT AEPIVPVDVK GKDAFHKLVD DLSAVLGPSS GLDSDDVDPK DIQKLMEGYV
SNHEEWQRYA LADESRAYTR NLVDEGNGKS NLLILVWNPG KSSPIHDHAN AHCVMKILHG
SLKEHRYDWP EQDKINNGEA CPLTVTKETI LRENEVAYMS DKLGLHKISN PDPNDFAISL
HLYTPPNAAH FGCSLFDEKT GKSHHIKQCT FFSNRGLKL
