ID   V093_FOWPN              Reviewed;          94 AA.
AC   Q9J5C7; O72895;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-NOV-2023, entry version 71.
DE   RecName: Full=Probable FAD-linked sulfhydryl oxidase FPV093;
DE            EC=1.8.3.2;
GN   OrderedLocusNames=FPV093; ORFNames=FPE10R;
OS   Fowlpox virus (strain NVSL) (FPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus; Fowlpox virus.
OX   NCBI_TaxID=928301;
OH   NCBI_TaxID=7742; Vertebrata.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FP-9 / Isolate HP-440;
RX   PubMed=9778782; DOI=10.1023/a:1008045914991;
RA   Pollitt E., Skinner M.A., Heaphy S.;
RT   "Nucleotide sequence of the 4.3 kbp BamHI-N fragment of fowlpox virus
RT   FP9.";
RL   Virus Genes 17:5-9(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT   "The genome of fowlpox virus.";
RL   J. Virol. 74:3815-3831(2000).
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   -!- SIMILARITY: Belongs to the poxviruses E10 family. {ECO:0000305}.
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DR   EMBL; AJ223385; CAA11288.1; -; Genomic_DNA.
DR   EMBL; AF198100; AAF44437.1; -; Genomic_DNA.
DR   RefSeq; NP_039056.1; NC_002188.1.
DR   SMR; Q9J5C7; -.
DR   GeneID; 1486641; -.
DR   KEGG; vg:1486641; -.
DR   Proteomes; UP000008597; Segment.
DR   GO; GO:0016972; F:thiol oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.20.120.310; ERV/ALR sulfhydryl oxidase domain; 1.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   InterPro; IPR006890; Sulphydryl_Oase_FAD-link_ERV1.
DR   Pfam; PF04805; Pox_E10; 1.
DR   PIRSF; PIRSF015696; VAC_E10R; 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; Oxidoreductase; Reference proteome.
FT   CHAIN           1..94
FT                   /note="Probable FAD-linked sulfhydryl oxidase FPV093"
FT                   /id="PRO_0000099467"
FT   DOMAIN          1..94
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   DISULFID        41..44
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   CONFLICT        8
FT                   /note="S -> R (in Ref. 1; CAA11288)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        11
FT                   /note="W -> G (in Ref. 1; CAA11288)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        41
FT                   /note="C -> R (in Ref. 1; CAA11288)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68..69
FT                   /note="FF -> SS (in Ref. 1; CAA11288)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   94 AA;  11252 MW;  401A36D5E96AAAF8 CRC64;
     MDPRYWGSSF WIVIFIIITK FKHDIETCKR HLYNICKALP CAECKDHALQ AIQKNNIMSS
     NDINYIYFFF ISLYNNLVFN PERCIDIKKV KKLI
//