ID   YR596_MIMIV             Reviewed;         292 AA.
AC   Q5UP54;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Probable FAD-linked sulfhydryl oxidase R596;
DE            EC=1.8.3.2;
GN   OrderedLocusNames=MIMI_R596;
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).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=16971431; DOI=10.1128/jvi.00940-06;
RA   Renesto P., Abergel C., Decloquement P., Moinier D., Azza S., Ogata H.,
RA   Fourquet P., Gorvel J.-P., Claverie J.-M., Raoult D.;
RT   "Mimivirus giant particles incorporate a large fraction of anonymous and
RT   unique gene products.";
RL   J. Virol. 80:11678-11685(2006).
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: Virion {ECO:0000269|PubMed:16971431}.
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DR   EMBL; AY653733; AAV50859.1; -; Genomic_DNA.
DR   RefSeq; YP_003987112.1; NC_014649.1.
DR   PDB; 3GWN; X-ray; 1.78 A; A/B=33-145.
DR   PDB; 3TD7; X-ray; 2.21 A; A=1-292.
DR   PDBsum; 3GWN; -.
DR   PDBsum; 3TD7; -.
DR   SMR; Q5UP54; -.
DR   GeneID; 9925233; -.
DR   KEGG; vg:9925233; -.
DR   OrthoDB; 14873at10239; -.
DR   EvolutionaryTrace; Q5UP54; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0044423; C:virion component; IEA:UniProtKB-KW.
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   Gene3D; 1.20.120.1250; Sulfhydryl oxidase R596, ORFan domain; 1.
DR   InterPro; IPR039799; ALR/ERV.
DR   InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR   InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR   InterPro; IPR049096; MIMI_R596-like_C.
DR   PANTHER; PTHR12645; ALR/ERV; 1.
DR   PANTHER; PTHR12645:SF0; FAD-LINKED SULFHYDRYL OXIDASE ALR; 1.
DR   Pfam; PF04777; Evr1_Alr; 1.
DR   Pfam; PF21491; MIMI_R596-like_C; 1.
DR   SUPFAM; SSF69000; FAD-dependent thiol oxidase; 1.
DR   PROSITE; PS51324; ERV_ALR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; FAD; Flavoprotein; Oxidoreductase;
KW   Reference proteome; Virion.
FT   CHAIN           1..292
FT                   /note="Probable FAD-linked sulfhydryl oxidase R596"
FT                   /id="PRO_0000247371"
FT   DOMAIN          33..139
FT                   /note="ERV/ALR sulfhydryl oxidase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   DISULFID        80..83
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT   HELIX           37..53
FT                   /evidence="ECO:0007829|PDB:3GWN"
FT   HELIX           61..77
FT                   /evidence="ECO:0007829|PDB:3GWN"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:3TD7"
FT   HELIX           81..90
FT                   /evidence="ECO:0007829|PDB:3GWN"
FT   HELIX           94..96
FT                   /evidence="ECO:0007829|PDB:3GWN"
FT   HELIX           100..103
FT                   /evidence="ECO:0007829|PDB:3GWN"
FT   HELIX           106..123
FT                   /evidence="ECO:0007829|PDB:3GWN"
FT   HELIX           132..140
FT                   /evidence="ECO:0007829|PDB:3GWN"
FT   HELIX           160..171
FT                   /evidence="ECO:0007829|PDB:3TD7"
FT   HELIX           180..183
FT                   /evidence="ECO:0007829|PDB:3TD7"
FT   HELIX           184..186
FT                   /evidence="ECO:0007829|PDB:3TD7"
FT   HELIX           187..192
FT                   /evidence="ECO:0007829|PDB:3TD7"
FT   HELIX           197..200
FT                   /evidence="ECO:0007829|PDB:3TD7"
FT   HELIX           201..208
FT                   /evidence="ECO:0007829|PDB:3TD7"
FT   TURN            209..211
FT                   /evidence="ECO:0007829|PDB:3TD7"
FT   HELIX           213..216
FT                   /evidence="ECO:0007829|PDB:3TD7"
FT   HELIX           221..238
FT                   /evidence="ECO:0007829|PDB:3TD7"
FT   TURN            249..252
FT                   /evidence="ECO:0007829|PDB:3TD7"
FT   HELIX           256..262
FT                   /evidence="ECO:0007829|PDB:3TD7"
FT   TURN            263..265
FT                   /evidence="ECO:0007829|PDB:3TD7"
FT   HELIX           271..290
FT                   /evidence="ECO:0007829|PDB:3TD7"
SQ   SEQUENCE   292 AA;  33998 MW;  5FEBA7FD1B7F526B CRC64;
     MSLSKQVVPT HRVEIAPNSE STCKMDHSNY QHNGLITKIW GTAGWTFNHA VTFGYPLNPT
     SDDKRRYKNY FISLGDVLPC RLCRESYKKF ITTGKTALTN EVLRNRHTLT KWFYDVHNAV
     NNKLEVDYGL SYEDVVNKYE SFRAKCGKPV PTVKGCVTPL DHKAFSFKKL YYMDAPIVSL
     DKVENFVRIA RMRGISDKYF CFLELATVLN GDFNELKKQS SWEYRNKYCQ KKIRHMRENA
     IPSIEEQGYW KGTPTIDELK LLLFLCSNLN RTEVNDAINN VERLESTHYI EN
//