UniProt: M1A5S1

Database: UniProt
Entry: M1A5S1_SOLTU

LinkDB:  M1A5S1_SOLTU 
Original site:  M1A5S1_SOLTU

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (11)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (3)   
Literature (1)   
   PubMed (1)   
All databases (17)   

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ID   M1A5S1_SOLTU            Unreviewed;       512 AA.
AC   M1A5S1;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE            EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN   Name=102582139 {ECO:0000313|EnsemblPlants:PGSC0003DMT400015284};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400015284, ECO:0000313|Proteomes:UP000011115};
RN   [1] {ECO:0000313|Proteomes:UP000011115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400015284}
RP   IDENTIFICATION.
RC   STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400015284};
RG   EnsemblPlants;
RL   Submitted (JUN-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   RefSeq; XP_006360420.1; XM_006360358.2.
DR   AlphaFoldDB; M1A5S1; -.
DR   EnsemblPlants; PGSC0003DMT400015284; PGSC0003DMT400015284; PGSC0003DMG400005962.
DR   GeneID; 102582139; -.
DR   Gramene; PGSC0003DMT400015284; PGSC0003DMT400015284; PGSC0003DMG400005962.
DR   OrthoDB; 20090at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; M1A5S1; baseline.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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:UP000011115};
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..512
FT                   /note="Sulfhydryl oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004011022"
FT   TRANSMEM        474..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU371123"
FT   DOMAIN          36..171
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          300..402
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000259|PROSITE:PS51324"
SQ   SEQUENCE   512 AA;  57791 MW;  6AB7A97534B8811E CRC64;
     MSCSIFLLFL ALFVSILEQS VSVSNGSQRE ILRAISGQDG EKPDFAVELN ATNFDSVLKE
     TPAPYAIVEF FAHWCPACRN YKPQYEKVAR LFNGANASHP GIILMTRVDC ALTINSNLCD
     KFSVKYYPML LWGPPKKFVG WDPKQENSEI LTIERGRTAD ILLGWINKQL GSSYGFDDEK
     YENEHLQRNF SDPGQIAKAI YDVEEATSTA FGIILDQRMI KSKTRASLIK FLQLLVAHHP
     SKRCRKGSAD ILVDFDNLCP SEILLAKNEA DSCSKKGTLG NYQICGEEVP RGYWMYCRGS
     KNDTRGFSCG LWVLLHSLSV RVEDGESDLA FRTTCDFIYN FFVCEECRQH FHGMCSSVSS
     PFKKARDFSL WLWSAHNQVN ERLMKDEESP GTGDPEFPKV TWPPKQLCPS CYLNPRKTSD
     ENSKIDWNEN EVFKFLVSYY GKELVNLYKD KELQAGGGTE KTVNEELVAS TNAVVVPLGA
     ALAIAVASCA FGALACFWRS QQKNRKPRRS WN
//

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