ID   FLSO_NPVAC              Reviewed;         259 AA.
AC   P41480;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   29-SEP-2021, entry version 56.
DE   RecName: Full=FAD-linked sulfhydryl oxidase;
DE   AltName: Full=p33;
DE            EC=1.8.3.2;
GN   Name=P33; ORFNames=ORF92;
OS   Autographa californica nuclear polyhedrosis virus (AcMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=46015;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6;
RX   PubMed=8030224; DOI=10.1006/viro.1994.1380;
RA   Ayres M.D., Howard S.C., Kuzio J., Lopez-Ferber M., Possee R.D.;
RT   "The complete DNA sequence of Autographa californica nuclear polyhedrosis
RT   virus.";
RL   Virology 202:586-605(1994).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9882325; DOI=10.1128/jvi.73.2.1227-1234.1999;
RA   Prikhod'ko G.G., Wang Y., Freulich E., Prives C., Miller L.K.;
RT   "Baculovirus p33 binds human p53 and enhances p53-mediated apoptosis.";
RL   J. Virol. 73:1227-1234(1999).
RN   [3]
RP   FUNCTION.
RX   PubMed=19409596; DOI=10.1016/j.virol.2009.04.006;
RA   Long C.M., Rohrmann G.F., Merrill G.F.;
RT   "The conserved baculovirus protein p33 (Ac92) is a flavin adenine
RT   dinucleotide-linked sulfhydryl oxidase.";
RL   Virology 388:231-235(2009).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 2-259, AND SUBUNIT.
RX   PubMed=21752922; DOI=10.1128/jvi.05149-11;
RA   Hakim M., Mandelbaum A., Fass D.;
RT   "Structure of a baculovirus sulfhydryl oxidase, a highly divergent member
RT   of the erv flavoenzyme family.";
RL   J. Virol. 85:9406-9413(2011).
CC   -!- FUNCTION: Functional FAD-linked sulfhydryl oxidase that is required for
CC       infectious budded virion (BV) production and for the formation of
CC       enveloped occluded virion (ODV). {ECO:0000269|PubMed:19409596}.
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   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21752922}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:9882325}. Host
CC       nucleus {ECO:0000269|PubMed:9882325}. Note=Shows a diffuse pattern of
CC       localization in the host cytoplasm and punctate localization in host
CC       nucleus. {ECO:0000269|PubMed:9882325}.
CC   -!- SIMILARITY: Belongs to the baculoviridae p33 family. {ECO:0000305}.
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DR   EMBL; L22858; AAA66722.1; -; Genomic_DNA.
DR   PIR; E72861; E72861.
DR   RefSeq; NP_054122.1; NC_001623.1.
DR   PDB; 3P0K; X-ray; 1.47 A; A=2-259.
DR   PDB; 3QZY; X-ray; 2.14 A; A/B=2-259.
DR   PDB; 5XKI; X-ray; 2.46 A; A/B=1-259.
DR   PDB; 5XTN; X-ray; 2.54 A; A/B/C/D=1-259.
DR   PDB; 5XTO; X-ray; 2.56 A; A/B/C/D=1-259.
DR   PDB; 5XTP; X-ray; 2.40 A; A/B/C/D=1-259.
DR   PDB; 5XTQ; X-ray; 2.04 A; A/B/C/D=1-259.
DR   PDB; 5XTR; X-ray; 2.25 A; A/B/C/D=1-259.
DR   PDBsum; 3P0K; -.
DR   PDBsum; 3QZY; -.
DR   PDBsum; 5XKI; -.
DR   PDBsum; 5XTN; -.
DR   PDBsum; 5XTO; -.
DR   PDBsum; 5XTP; -.
DR   PDBsum; 5XTQ; -.
DR   PDBsum; 5XTR; -.
DR   SMR; P41480; -.
DR   GeneID; 1403925; -.
DR   KEGG; vg:1403925; -.
DR   BRENDA; 1.8.3.2; 583.
DR   Proteomes; UP000008292; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016972; F:thiol oxidase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR007879; Baculo_p33.
DR   Pfam; PF05214; Baculo_p33; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Early protein; Host cytoplasm; Host nucleus; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..259
FT                   /note="FAD-linked sulfhydryl oxidase"
FT                   /id="PRO_0000132896"
FT   HELIX           6..24
FT                   /evidence="ECO:0007829|PDB:3P0K"
FT   HELIX           25..28
FT                   /evidence="ECO:0007829|PDB:3P0K"
FT   HELIX           32..54
FT                   /evidence="ECO:0007829|PDB:3P0K"
FT   HELIX           59..71
FT                   /evidence="ECO:0007829|PDB:3P0K"
FT   HELIX           78..91
FT                   /evidence="ECO:0007829|PDB:3P0K"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:3P0K"
FT   HELIX           106..125
FT                   /evidence="ECO:0007829|PDB:3P0K"
FT   TURN            126..128
FT                   /evidence="ECO:0007829|PDB:3P0K"
FT   HELIX           129..131
FT                   /evidence="ECO:0007829|PDB:3QZY"
FT   HELIX           132..147
FT                   /evidence="ECO:0007829|PDB:3P0K"
FT   HELIX           156..165
FT                   /evidence="ECO:0007829|PDB:3P0K"
FT   HELIX           167..184
FT                   /evidence="ECO:0007829|PDB:3P0K"
FT   STRAND          190..193
FT                   /evidence="ECO:0007829|PDB:3P0K"
FT   HELIX           195..202
FT                   /evidence="ECO:0007829|PDB:3P0K"
FT   STRAND          204..207
FT                   /evidence="ECO:0007829|PDB:3P0K"
FT   STRAND          211..213
FT                   /evidence="ECO:0007829|PDB:3P0K"
FT   HELIX           216..235
FT                   /evidence="ECO:0007829|PDB:3P0K"
FT   HELIX           249..256
FT                   /evidence="ECO:0007829|PDB:3P0K"
SQ   SEQUENCE   259 AA;  30937 MW;  2EA816E747D9A9B3 CRC64;
     MIPLTPLFSR YKDSYLLYSF RLIDLLRASK STHLTKLLSS QATYLYHFAC LMKYKDIQKY
     EVQQLIEWAI NASPDMDLQQ FRIEFMDKTT ELNLRSCQPK SFTYTFTTIW DTMHFLSLII
     DDMVYTRDKS SLDFVMQQLK TMKVLFYNVF FILQCAMCRD HYMNVKGFII YHIELIEIAL
     DKEKYGTDIT FVDSYQQETA GADVAVVSNN MLMKNLMAYV SMTFHNHIND YKWIQRNKKP
     PAHYERMTWG EYKKLLNLQ