ID   E10_VACCC               Reviewed;          95 AA.
AC   P21050;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Probable FAD-linked sulfhydryl oxidase E10;
DE            EC=1.8.3.2;
GN   ORFNames=E10R;
OS   Vaccinia virus (strain Copenhagen) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "The complete DNA sequence of vaccinia virus.";
RL   Virology 179:247-266(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL   Virology 179:517-563(1990).
CC   -!- FUNCTION: FAD-dependent sulfhydryl oxidase that catalyzes disulfide
CC       bond formation. The complete pathway for formation of disulfide bonds
CC       in intracellular virion membrane proteins sequentially involves
CC       oxidation of E10, A2.5 and G4 (By similarity). {ECO:0000255|PROSITE-
CC       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;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00654};
CC   -!- SUBUNIT: Interacts with A2.5; this interaction involves formation of a
CC       transient disulfide-bonded intermediate, allowing disulfide bond
CC       transfer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}. Note=Associated with crescent
CC       membranes, immature virions (IV) and mature virions (MV).
CC       {ECO:0000250}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC   -!- SIMILARITY: Belongs to the poxviridae E10 family. {ECO:0000305}.
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DR   EMBL; M35027; AAA48051.1; -; Genomic_DNA.
DR   PIR; E42509; E42509.
DR   SMR; P21050; -.
DR   PRIDE; P21050; -.
DR   Proteomes; UP000008269; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016972; F:thiol oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.20.120.310; -; 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; SSF69000; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; FAD; Flavoprotein; Late protein; Membrane; Oxidoreductase;
KW   Redox-active center; Reference proteome; Transmembrane;
KW   Transmembrane helix; Viral envelope protein; Virion.
FT   CHAIN           1..95
FT                   /note="Probable FAD-linked sulfhydryl oxidase E10"
FT                   /id="PRO_0000099464"
FT   TOPO_DOM        1..8
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..95
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1..95
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   DISULFID        43..46
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
SQ   SEQUENCE   95 AA;  10851 MW;  F4A2FDC41599EA50 CRC64;
     MNPKHWGRAV WTIIFIVLSQ AGLDGNIEAC KRKLYTIVST LPCPACRRHA TIAIEDNNVM
     SSDDLNYIYY FFIRLFNNLA SDPKYAIDVS KVKPL