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Database: UniProt
Entry: A0A182FF50_ANOAL
LinkDB: A0A182FF50_ANOAL
Original site: A0A182FF50_ANOAL 
ID   A0A182FF50_ANOAL        Unreviewed;       713 AA.
AC   A0A182FF50;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Sulfhydryl oxidase {ECO:0000256|RuleBase:RU371123};
DE            EC=1.8.3.2 {ECO:0000256|RuleBase:RU371123};
OS   Anopheles albimanus (New world malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7167 {ECO:0000313|EnsemblMetazoa:AALB005142-PA, ECO:0000313|Proteomes:UP000069272};
RN   [1] {ECO:0000313|EnsemblMetazoa:AALB005142-PA}
RP   IDENTIFICATION.
RC   STRAIN=STECLA/ALBI9_A {ECO:0000313|EnsemblMetazoa:AALB005142-PA};
RG   EnsemblMetazoa;
RL   Submitted (AUG-2022) 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};
CC   -!- SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX) family.
CC       {ECO:0000256|ARBA:ARBA00006041}.
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DR   AlphaFoldDB; A0A182FF50; -.
DR   STRING; 7167.A0A182FF50; -.
DR   EnsemblMetazoa; AALB005142-RA; AALB005142-PA; AALB005142.
DR   VEuPathDB; VectorBase:AALB005142; -.
DR   VEuPathDB; VectorBase:AALB20_026075; -.
DR   Proteomes; UP000069272; Chromosome 3L.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016971; F:flavin-dependent sulfhydryl oxidase activity; IEA:InterPro.
DR   CDD; cd02992; PDI_a_QSOX; 1.
DR   Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.20.120.1960; QSOX sulfhydryl oxidase domain; 1.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   InterPro; IPR040986; QSOX_FAD-bd_dom.
DR   InterPro; IPR042568; QSOX_FAD-bd_sf.
DR   InterPro; IPR039798; Sulfhydryl_oxidase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
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; PF18371; FAD_SOX; 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; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
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   Transmembrane {ECO:0000256|RuleBase:RU371123};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU371123}.
FT   TRANSMEM        672..690
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU371123"
SQ   SEQUENCE   713 AA;  79859 MW;  AD31910FCA20A2F5 CRC64;
     MVRNSVGAPC VRQRPSGSCT STLLLLLLVA TVVDVGPRLA PVHGGLTGGR GGGGLRDKLS
     IYEQRRFARQ IEEQENSGLY DSSDSVISLT AANLKERVYN QPHASLVEFY NSYCGFCRRF
     APIWKQLAAD ILGWQTLVKV TALDCSREEN NAICREYEVM AYPTIRFFAP HYTDGEQKIG
     EPLKEHDGPR ILDRLVEFMA RVENKPATWP NLTTINQTTD DKASLFVEGA GTASAKPRYV
     YLVNEKDANG TIGLQVVLDF HDTPGVAVYR VHGDPAVAAT DSNNLSVIDG SSLSLIRLPI
     DEFTREKVRE AIRAHLRQHH IIVTDVTTKS TTTKAGGQGG DGQPSEQSIS ALMEQKQEQA
     IRAKVKELGA GVVYQADLEE AIRFALFREV ARFKTIDGER LAALRHFLDV LVRYFPFNDN
     GQRFLTELRQ YVLNAGETSL DGQAFVERAK ALEQERSPVF ASNHWIGCSG SKEGLRRYPC
     GLWTLFHYLA VQAAENDRAT NAQEVLEAMH GYIKHFFGCT ECSQHFQQMA EKNRIWQVAT
     KEDAILWLWS SHNEVNKRLA GDATEDPEHP KVQFPPVSDC PQCRKKILTN HHNHKQYTME
     DGNEWDLTEV LRYLQHMYAY ERRNLFGLHD SSLAPKAERD GGREGAAAAA AAQTSYHSYG
     NVLSDIDIRF SALLYITCIV MIVIAIKMVV KRGYRKKLYP HDILGKVAPV VMG
//
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