(data stored in SCRATCH zone)

SWISSPROT: Q75BU6_ASHGO

ID   Q75BU6_ASHGO            Unreviewed;       198 AA.
AC   Q75BU6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 91.
DE   RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE            EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
GN   ORFNames=AGOS_ACR175W {ECO:0000313|EMBL:AAS51401.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51401.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51401.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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|RuleBase:RU371123};
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DR   EMBL; AE016816; AAS51401.1; -; Genomic_DNA.
DR   RefSeq; NP_983577.1; NM_208930.1.
DR   STRING; 33169.AAS51401; -.
DR   EnsemblFungi; AAS51401; AAS51401; AGOS_ACR175W.
DR   GeneID; 4619709; -.
DR   KEGG; ago:AGOS_ACR175W; -.
DR   HOGENOM; HOG000180458; -.
DR   InParanoid; Q75BU6; -.
DR   KO; K17891; -.
DR   OMA; ECAGHFR; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; IBA:GO_Central.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IBA:GO_Central.
DR   Gene3D; 1.20.120.310; -; 1.
DR   InterPro; IPR039799; ALR/ERV.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   PANTHER; PTHR12645; PTHR12645; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   SUPFAM; SSF69000; SSF69000; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
PE   4: Predicted;
DR   PRODOM; Q75BU6.
DR   SWISS-2DPAGE; Q75BU6.
KW   FAD {ECO:0000256|RuleBase:RU371123};
KW   Flavoprotein {ECO:0000256|RuleBase:RU371123};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU371123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          70..173
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000259|PROSITE:PS51324"
SQ   SEQUENCE   198 AA;  21871 MW;  2A4CD2663F0EFA5F CRC64;
     MKLHRQKVLS IVAAAAIVGL WYMFFGQQLS NRETYDPDVV PQQEGRTPAA VRAAADKNQA
     PMIKGSIMPG MPDPTAKQEL GRATWKLFHT MLARFPDEPS EQEREKLHTF LHLLAELYPC
     GECSVHFVSW LKKLPPQTSS RSAAATWGCS IHNKVNLYLG KPAYDCSKIL EDYDCGCGDD
     AAAGSLKVSV HTERPQGG
//

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