ID A0A0N5BNF7_STREA Unreviewed; 579 AA.
AC A0A0N5BNF7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000743600.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0000743600.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) 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; A0A0N5BNF7; -.
DR STRING; 174720.A0A0N5BNF7; -.
DR WBParaSite; SPAL_0000743600.1; SPAL_0000743600.1; SPAL_0000743600.
DR Proteomes; UP000046392; Unplaced.
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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..579
FT /note="Sulfhydryl oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005894856"
FT DOMAIN 16..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 579 AA; 67351 MW; 8F9205DBA988AB66 CRC64;
MQAYYIKLFL SFILLLRSCT LAEVANHTTQ PNGSHGTLYT NEDYVIQLDT NTFNDTIYCN
GQEDCSAFIV EFYADWCGHC RNYAPMYIDL ADDIKKWKNV IKLAAINCAD TYNLPVCTAH
NIRSLPTIKY FEKNSRSTDN GLKFKAYHNI ASMRKQITEY VIREQHTKKY ENWPDFNYIG
DISRFSQLWT GLNENISTMA ILFDNEKDDL LGSLILLDLS YYSNKVAIRR SDKHHPLAAA
FDIQNFPAVV IIKRGEKKPI FVSDFRKMIS NDFESFFNAD SMVESIINRT PERINRTSVD
CNTSPELCKP KYYVSESDML KAIKYALTNE IELVGKNLTG NSLTALFNFI NMLNDHYPGY
TTNGSDNSDV QILDNSSRAK QIFFNLKQFL TTKMMENSLA LDDWISEFKK FESKFENPFA
DDVDWDHCKG TETRYRGYTC GLWTLFHTIT VSAFNNAPTE GEFDPIPIIY SIRGWVGEFF
GCEFCRKHFL DMTGRKYKIE DHIKTKDDTY LYLWRAHNIV NKRIKGDDSE DPNFKKYQFP
AKFLCKECNE ESESLDNPKT HKFIQTYYSN IKPYVKQTN
//
