CDO_CANAL
ID CDO_CANAL Reviewed; 265 AA.
AC Q5A3Z5; A0A1D8PTW3;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cysteine dioxygenase CDG1;
DE Short=CDO;
DE EC=1.13.11.20;
GN Name=CDG1; OrderedLocusNames=CAALFM_CR09180WA; ORFNames=CaO19.7314;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP INDUCTION.
RX PubMed=12397174; DOI=10.1073/pnas.232566499;
RA Lan C.Y., Newport G., Murillo L.A., Jones T., Scherer S., Davis R.W.,
RA Agabian N.;
RT "Metabolic specialization associated with phenotypic switching in
RT Candidaalbicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14907-14912(2002).
RN [5]
RP INDUCTION.
RX PubMed=19527170; DOI=10.1086/599838;
RA Nett J.E., Lepak A.J., Marchillo K., Andes D.R.;
RT "Time course global gene expression analysis of an in vivo Candida
RT biofilm.";
RL J. Infect. Dis. 200:307-313(2009).
RN [6]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23417561; DOI=10.1128/ec.00336-12;
RA Hennicke F., Grumbt M., Lermann U., Ueberschaar N., Palige K., Bottcher B.,
RA Jacobsen I.D., Staib C., Morschhauser J., Monod M., Hube B., Hertweck C.,
RA Staib P.;
RT "Factors supporting cysteine tolerance and sulfite production in Candida
RT albicans.";
RL Eukaryot. Cell 12:604-613(2013).
CC -!- FUNCTION: Cysteine dioxygenase involved in sulfite formation from
CC cysteine. Plays an important role in filamentous growth and virulence.
CC {ECO:0000269|PubMed:23417561}.
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- INDUCTION: Expression is under the control of the ZCF2 transcription
CC factor and is regulated upon white-opaque switching. Transcription is
CC also up-regulated in both intermediate and mature biofilms.
CC {ECO:0000269|PubMed:12397174, ECO:0000269|PubMed:19527170,
CC ECO:0000269|PubMed:23417561}.
CC -!- PTM: The thioether cross-link between Cys-157 and Tyr-221 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: Displays reduced hyphae formation in the presence
CC of cysteine and leads to attenuated virulence.
CC {ECO:0000269|PubMed:23417561}.
CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family. {ECO:0000305}.
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DR EMBL; CP017630; AOW31583.1; -; Genomic_DNA.
DR RefSeq; XP_716448.1; XM_711355.1.
DR AlphaFoldDB; Q5A3Z5; -.
DR SMR; Q5A3Z5; -.
DR STRING; 237561.Q5A3Z5; -.
DR GeneID; 3641883; -.
DR KEGG; cal:CAALFM_CR09180WA; -.
DR CGD; CAL0000188872; CDG1.
DR VEuPathDB; FungiDB:CR_09180W_A; -.
DR eggNOG; KOG4064; Eukaryota.
DR HOGENOM; CLU_079443_4_0_1; -.
DR InParanoid; Q5A3Z5; -.
DR OMA; WPDRKSH; -.
DR OrthoDB; 1516232at2759; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0017172; F:cysteine dioxygenase activity; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0019448; P:L-cysteine catabolic process; IBA:GO_Central.
DR GO; GO:0019451; P:L-cysteine catabolic process to pyruvate, using cysteine dioxygenase; IMP:CGD.
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 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Thioether bond; Virulence.
FT CHAIN 1..265
FT /note="Cysteine dioxygenase CDG1"
FT /id="PRO_0000422071"
FT REGION 14..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 150
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q16878"
FT BINDING 152
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q16878"
FT BINDING 204
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q16878"
FT CROSSLNK 157..221
FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:Q16878"
SQ SEQUENCE 265 AA; 29798 MW; 3E5AA4A66919F4BF CRC64;
MLLNQYTFSA ERCTTPTSIS HPPLACPTSP PPTNSLNRYQ HKPVTLAPTV DHGCEINGTT
IDCIPKDSKF YQLIMDLKQL LAGKGLSNED IDVEKVKQLM ADYDSNEIDW QHLALHDPSR
NYSRNGIINL NGNANLLILV WSPGKSSAIH DHADAHCCVK MLAGELIEHL YDFPDHEGEE
LQCRQETSMK RNDVGYINDS IGLHKMSNPL QNRVSVSLHL YTPPYASMYG CSMYEASSGR
KHHVDMSKYY SWQGQLVNEK ESSTC
