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Database: UniProt
Entry: D0P4F0_PHYIT
LinkDB: D0P4F0_PHYIT
Original site: D0P4F0_PHYIT 
ID   D0P4F0_PHYIT            Unreviewed;       398 AA.
AC   D0P4F0;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE            EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN   ORFNames=PITG_21553 {ECO:0000313|EMBL:EEY65304.1};
OS   Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY65304.1, ECO:0000313|Proteomes:UP000006643};
RN   [1] {ECO:0000313|Proteomes:UP000006643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX   PubMed=19741609; DOI=10.1038/nature08358;
RG   The Broad Institute Genome Sequencing Platform;
RA   Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA   Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA   Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA   Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA   Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA   Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA   Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA   Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA   Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA   Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA   Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA   Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA   Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA   Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA   Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA   Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA   Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA   Nusbaum C.;
RT   "Genome sequence and analysis of the Irish potato famine pathogen
RT   Phytophthora infestans.";
RL   Nature 461:393-398(2009).
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; DS028587; EEY65304.1; -; Genomic_DNA.
DR   RefSeq; XP_002894825.1; XM_002894779.1.
DR   AlphaFoldDB; D0P4F0; -.
DR   EnsemblProtists; PITG_21553T0; PITG_21553T0; PITG_21553.
DR   GeneID; 9477820; -.
DR   KEGG; pif:PITG_21553; -.
DR   VEuPathDB; FungiDB:PITG_21553; -.
DR   eggNOG; KOG0191; Eukaryota.
DR   eggNOG; KOG1731; Eukaryota.
DR   HOGENOM; CLU_556081_0_0_1; -.
DR   InParanoid; D0P4F0; -.
DR   OMA; CREYKAD; -.
DR   OrthoDB; 64317at2759; -.
DR   Proteomes; UP000006643; Partially assembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; IEA:InterPro.
DR   CDD; cd02961; PDI_a_family; 1.
DR   Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
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:SF8; SULFHYDRYL OXIDASE; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
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}; Membrane {ECO:0000256|RuleBase:RU371123};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU371123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006643};
KW   Transmembrane {ECO:0000256|RuleBase:RU371123};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT   TRANSMEM        361..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU371123"
FT   DOMAIN          1..101
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          206..335
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000259|PROSITE:PS51324"
SQ   SEQUENCE   398 AA;  45616 MW;  C1E00A6EDE126DA0 CRC64;
     MLNDTQTVWL VDFYSPWCPH CRQFAPQWEE VANVYAKVKT IQLGAVDCTK QNEICGREDV
     HSYPAVKMFH VPPDSIEAIE MPHDDHVYAR HVAKWIEETL KEHGMGPFID VDKVYPKNTM
     RNDLKKKEFK FGDPVEPLYD DRSAEIQLKR LKDAGTTALF VLKDGFFMGT TELAGERYAA
     AVTWVQTLAN AFPTKENRAA FVLLVDMMKK QSRWKQADWN TMLDNWKVSA NAISYPTNLF
     ASKDELSLCT TFTCGLWTLE IMIAIRLVVK HFFGCEECKR HFLKANPESL IEKLALRDED
     GSDAVAFWIW TMHNTVNKVL SKPRWPTNLS CPNCYFANDQ PPSLDPAQLS EEDIVAYVKR
     FTSMAAVALL IAIFATIFQQ HKHRLAGMKV LKTRDHIA
//
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