ID A0A225WLP3_9STRA Unreviewed; 486 AA.
AC A0A225WLP3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN ORFNames=PHMEG_0008058 {ECO:0000313|EMBL:OWZ17937.1};
OS Phytophthora megakarya.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4795 {ECO:0000313|EMBL:OWZ17937.1, ECO:0000313|Proteomes:UP000198211};
RN [1] {ECO:0000313|Proteomes:UP000198211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=zdho120 {ECO:0000313|Proteomes:UP000198211};
RA Ali S., Shao J., Larry D.J., Kronmiller B., Shen D., Strem M.D.,
RA Melnick R.L., Guiltinan M.J., Tyler B.M., Meinhardt L.W., Bailey B.A.;
RT "Phytopthora megakarya and P. palmivora, two closely related causual agents
RT of cacao black pod achieved similar genome size and gene model numbers by
RT different mechanisms.";
RL Submitted (MAR-2017) 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:OWZ17937.1}.
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DR EMBL; NBNE01000668; OWZ17937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225WLP3; -.
DR EnsemblProtists; OWZ17937; OWZ17937; PHMEG_0008058.
DR OrthoDB; 64317at2759; -.
DR Proteomes; UP000198211; Unassembled 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:UP000198211};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|RuleBase:RU371123};
KW Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..486
FT /note="Sulfhydryl oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012533546"
FT TRANSMEM 443..466
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU371123"
FT DOMAIN 27..150
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 293..398
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000259|PROSITE:PS51324"
SQ SEQUENCE 486 AA; 55473 MW; 37592651F4425113 CRC64;
MRGLLLSSVA LFTSGWLSSV SAFRPRPDGG ELFETTKVVR SLDTDTFNAM LNDTKTVWLV
DFYSPWCPHC RQFAPQWEEV GKVYADVDAI QLGAVDCTRQ NEICDQEGVH NYPGVKMYHV
PSTATEAIDM PHAGHIYARH VAKWIEETLR ENDMQSGIDI DKVYTRNPLH SDLKKKEFKF
GDPVEPLHDD RSEDIQLKRL KDAGATALLT FEDGFFMGMT VLEDERYEAA VTWVKTLVAT
FPMKENRAVL AVLLEKMKQQ EKWKLSEWKE MLATWQMTAN AMSFPVNLFA SDEKLALCTT
YTCGLWTLFH SLTVNVSQLK PSEVMSAIRL VVKHFFGCEE CKRHFLKANP ESVVTKLALR
DEDGPEAVVL WIWTMHNTVN KVLSKPMWPT KLSCPFCYSP GDLPLSLDPK QLNEDDIFEY
VRDVYKIETN LKFAQHFASS TTWFSMGGFT SMATIAILVA IFVMVFQQHK HRLVGMKALK
TRDHIA
//
