ID   G0T168_RHOT2            Unreviewed;       199 AA.
AC   G0T168;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   08-NOV-2023, entry version 41.
DE   RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE            EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN   ORFNames=RTG_02868 {ECO:0000313|EMBL:EGU11367.1};
OS   Rhodosporidium toruloides (strain ATCC 204091 / IIP 30 / MTCC 1151) (Yeast)
OS   (Rhodotorula glutinis (strain ATCC 204091)).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1001064 {ECO:0000313|EMBL:EGU11367.1, ECO:0000313|Proteomes:UP000006141};
RN   [1] {ECO:0000313|EMBL:EGU11367.1, ECO:0000313|Proteomes:UP000006141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204091 / IIP 30 / MTCC 1151
RC   {ECO:0000313|Proteomes:UP000006141};
RX   PubMed=24526636; DOI=10.1128/genomeA.00046-14;
RA   Paul D., Magbanua Z., Arick M.II., French T., Bridges S.M., Burgess S.C.,
RA   Lawrence M.L.;
RT   "Genome sequence of the oleaginous yeast Rhodotorula glutinis ATCC
RT   204091.";
RL   Genome Announc. 2:E0004614-E0004614(2014).
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};
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:EGU11367.1}.
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; AEVR02000018; EGU11367.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0T168; -.
DR   HOGENOM; CLU_070631_1_0_1; -.
DR   InParanoid; G0T168; -.
DR   Proteomes; UP000006141; 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:SF0; FAD-LINKED SULFHYDRYL OXIDASE ALR; 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:UP000006141}.
FT   DOMAIN          85..188
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000259|PROSITE:PS51324"
SQ   SEQUENCE   199 AA;  20812 MW;  3A20ABE595EEFBB6 CRC64;
     MTETAGGALP PGMVIGPDGK PCKACTAFRS FAGFKKKPGT QSSAGGDAFA AGTPSSTSSA
     AGVVAAGAAL AGVTAAAEPV LPADCPPDVE RLGRHTWTFL HTTASYFPPQ PSQHQKSSML
     GLLRALPTLY PCGVCADHLG QYMKTHPPEA AVEKGREALE GWLCNVHNEV NERLGKDKFN
     CANVPQRWRD GWADGHCDP
//