ID   YR368_MIMIV             Reviewed;         143 AA.
AC   Q5UQV6;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Probable FAD-linked sulfhydryl oxidase R368;
DE            EC=1.8.3.2;
GN   OrderedLocusNames=MIMI_R368;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Megamimivirinae; Mimivirus;
OC   Mimivirus bradfordmassiliense.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- FUNCTION: FAD-dependent sulfhydryl oxidase that catalyzes disulfide
CC       bond formation. {ECO:0000255|PROSITE-ProRule:PRU00654}.
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00654};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; AY653733; AAV50637.1; -; Genomic_DNA.
DR   RefSeq; YP_003986873.1; NC_014649.1.
DR   SMR; Q5UQV6; -.
DR   GeneID; 9924989; -.
DR   KEGG; vg:9924989; -.
DR   OrthoDB; 14873at10239; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   InterPro; IPR039799; ALR/ERV.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   PANTHER; PTHR12645; ALR/ERV; 1.
DR   PANTHER; PTHR12645:SF0; FAD-LINKED SULFHYDRYL OXIDASE ALR; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; FAD; Flavoprotein; Membrane; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..143
FT                   /note="Probable FAD-linked sulfhydryl oxidase R368"
FT                   /id="PRO_0000309199"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          10..104
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   DISULFID        46..49
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
SQ   SEQUENCE   143 AA;  16981 MW;  CA9BCD24A6933889 CRC64;
     MSPEQWGIYG WTFSHAVALG YPINPTEEDK LRYYTFFNSY RYVLPCGKCR INYADHLNKY
     PLTDEVLSSR ENLVKWTIDI HNVVNYYTGK KMLTYPEAIE AIEKTLTPKK KSSYNWFFII
     LIIIGIIVII YLMYIVFKKK LNK
//