ID   A0A0D7BNQ0_9AGAR        Unreviewed;       220 AA.
AC   A0A0D7BNQ0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-NOV-2023, entry version 24.
DE   RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE            EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN   ORFNames=CYLTODRAFT_98900 {ECO:0000313|EMBL:KIY71815.1};
OS   Cylindrobasidium torrendii FP15055 ss-10.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC   Cylindrobasidium.
OX   NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY71815.1, ECO:0000313|Proteomes:UP000054007};
RN   [1] {ECO:0000313|EMBL:KIY71815.1, ECO:0000313|Proteomes:UP000054007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY71815.1,
RC   ECO:0000313|Proteomes:UP000054007};
RX   PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA   Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA   Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA   LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA   Hibbett D.S.;
RT   "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT   genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL   Fungal Genet. Biol. 76:78-92(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR';
CC         Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2;
CC         Evidence={ECO:0000256|RuleBase:RU371123};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU371123};
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DR   EMBL; KN880450; KIY71815.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D7BNQ0; -.
DR   STRING; 1314674.A0A0D7BNQ0; -.
DR   OrthoDB; 1265at2759; -.
DR   Proteomes; UP000054007; Unassembled WGS sequence.
DR   GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; IEA:InterPro.
DR   Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR   InterPro; IPR039799; ALR/ERV.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   PANTHER; PTHR12645; ALR/ERV; 1.
DR   PANTHER; PTHR12645:SF1; FAD-LINKED SULFHYDRYL OXIDASE ERV2; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU371123};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU371123};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU371123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054007}.
FT   DOMAIN          81..181
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000259|PROSITE:PS51324"
SQ   SEQUENCE   220 AA;  24416 MW;  0915A8A0027E7490 CRC64;
     MAKIISRFAK SFFAVIAALF LLATVLFFHP PMRAYIDPWT GDVFGEGGVE QYFKAATPTE
     KVHSLNKGSV HGEVIMPKLG NATAKAALGR ATWKLLHTMT LRYPETPSPD EREALDSYFH
     LLSRLYPCGE CAAEFQQLLA KYPPQTSSRK AASLWLCDVH NKVNKRLGHA QFDCAHLDAE
     YDCGCGDEPI INTKEPDDME NELPPDADEL TGVKMIKGGR
//