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Database: UniProt
Entry: A0A179HXQ1_PURLI
LinkDB: A0A179HXQ1_PURLI
Original site: A0A179HXQ1_PURLI 
ID   A0A179HXQ1_PURLI        Unreviewed;       220 AA.
AC   A0A179HXQ1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE            EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN   ORFNames=PLICBS_000494 {ECO:0000313|EMBL:GJN66476.1}, VFPBJ_01393
GN   {ECO:0000313|EMBL:OAQ87353.1}, VFPFJ_01415
GN   {ECO:0000313|EMBL:OAQ95305.1};
OS   Purpureocillium lilacinum (Paecilomyces lilacinus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX   NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ95305.1, ECO:0000313|Proteomes:UP000078340};
RN   [1] {ECO:0000313|EMBL:OAQ95305.1, ECO:0000313|Proteomes:UP000078340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PLBJ-1 {ECO:0000313|EMBL:OAQ87353.1}, and PLFJ-1
RC   {ECO:0000313|EMBL:OAQ95305.1};
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT   Phytophthora in bio-control Purpureocillium lilacinum.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GJN66476.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 284.36 {ECO:0000313|EMBL:GJN66476.1};
RA   Alimu Y., Kusuya Y., Yamamoto T., Shigemune N., Takahashi H., Yaguchi T.;
RT   "Tolerabce induction of polyhexamethylene biguanide on Purpureocillium
RT   lilacinum strains.";
RL   Submitted (DEC-2021) to the EMBL/GenBank/DDBJ databases.
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:OAQ95305.1}.
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DR   EMBL; BQKW01000001; GJN66476.1; -; Genomic_DNA.
DR   EMBL; LSBH01000001; OAQ87353.1; -; Genomic_DNA.
DR   EMBL; LSBI01000001; OAQ95305.1; -; Genomic_DNA.
DR   RefSeq; XP_018184024.1; XM_018318499.1.
DR   STRING; 33203.A0A179HXQ1; -.
DR   GeneID; 28883548; -.
DR   KEGG; plj:VFPFJ_01415; -.
DR   OMA; PLFDCEN; -.
DR   OrthoDB; 1265at2759; -.
DR   Proteomes; UP000078240; Unassembled WGS sequence.
DR   Proteomes; UP000078340; Unassembled WGS sequence.
DR   Proteomes; UP001056679; 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:UP000078340}.
FT   DOMAIN          86..186
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000259|PROSITE:PS51324"
FT   REGION          192..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   220 AA;  24136 MW;  B5C18C3D39F9A59E CRC64;
     MARRQHLTAS LILALVVFFS ITFFMTGSST AGRNVADLSP GAARSAPEKP LKGLDTPHDG
     ASSFAVDLES AGDLFNGDSI APKMENATLK AELGRATWRF LHTMVARFPE KPTPDDRKTL
     ETFIHLFARL YPCGDCAKHF RGLLAKYPPQ TSSRNSAAGW LCFAHNVVNE RLHKPVFDCN
     KIGDFYDCGC GDEGKKDKKK EGEKRDEDAL ATSEIKAEAL
//
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