ID A0A0K0ER31_STRER Unreviewed; 577 AA.
AC A0A0K0ER31;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0001191300.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0001191300.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
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 AlphaFoldDB; A0A0K0ER31; -.
DR STRING; 6248.A0A0K0ER31; -.
DR WBParaSite; SSTP_0001191300.1; SSTP_0001191300.1; SSTP_0001191300.
DR Proteomes; UP000035681; 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 Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR Gene3D; 1.20.120.1960; QSOX sulfhydryl oxidase domain; 1.
DR InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR InterPro; IPR042568; QSOX_FAD-bd_sf.
DR InterPro; IPR039798; Sulfhydryl_oxidase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR22897; QUIESCIN Q6-RELATED SULFHYDRYL OXIDASE; 1.
DR PANTHER; PTHR22897:SF27; SULFHYDRYL OXIDASE; 1.
DR Pfam; PF04777; Evr1_Alr; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51324; ERV_ALR; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 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:UP000035681};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..577
FT /note="Sulfhydryl oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005328473"
FT DOMAIN 27..162
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 431..539
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000259|PROSITE:PS51324"
SQ SEQUENCE 577 AA; 67503 MW; F4B762E0963872D8 CRC64;
MQMYYIKIFI SIFLLHITCI LAEVANHTTE PKGTHATLYT SEDYVIQLDT TTFNDTVYCD
GQKDCSAFIV EFYADWCGHC RNYAPMYIEL AEDIKKWKNV IKLAAINCAD TYNLPICTTH
SIRSLPTIKY FEKNSKILDN GIKFKAYHNI ASMRKQITEY VIREQHTKKY DNWPDFEYIG
DIGRFSELWA GLNENISTMA ILFDNEKNDL LGSLILLDLS YYSDKVIIKR SDKNHPLATV
FDIQNFPAVA IIKRGEKKPI FVSDFRKMIS GELESFFNAD NMVETIINRT PERHNRSSID
CNTSPELCKP KYFVSEIDML KAIKYSLTNE IELVGQNLTN NSLTALYNYV NMLNDHYPGY
TTNGSDNTDV QILDNSSKAK QIFFNLKQFL TTKMMENFLT LSDWTNEFKK YEKKFDNPFA
DDVDWEHCKG TEPRYRGYTC GLWTLFHTIT VSAYKNAPLN EEFDPIPIIY SIKGWVGEFF
GCEYCRKHFL DMTGRKFKIE DHIKTKEDTY LYLWKAHNIV NNRIKGYDSE DPNFKKYQFP
AKFLCKECNE DFESLDNPKT SKFLQDYYSN IKPYVKN
//
