FLSO_ASFB7
ID FLSO_ASFB7 Reviewed; 119 AA.
AC Q65163;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=FAD-linked sulfhydryl oxidase {ECO:0000303|PubMed:16537584};
DE EC=1.8.3.2 {ECO:0000269|PubMed:16537584};
DE AltName: Full=p14;
GN OrderedLocusNames=Ba71V-073; ORFNames=9GL, B119L;
OS African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10498;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA Rodriguez J.F., Vinuela E.;
RT "Analysis of the complete nucleotide sequence of African swine fever
RT virus.";
RL Virology 208:249-278(1995).
RN [2]
RP CHARACTERIZATION.
RX PubMed=10627538; DOI=10.1128/jvi.74.3.1275-1285.2000;
RA Lewis T., Zsak L., Burrage T.G., Lu Z., Kutish G.F., Neilan J.G.,
RA Rock D.L.;
RT "An African swine fever virus ERV1-ALR homologue, 9GL, affects virion
RT maturation and viral growth in macrophages and viral virulence in swine.";
RL J. Virol. 74:1275-1285(2000).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH A151R, AND CATALYTIC
RP ACTIVITY.
RX PubMed=16537584; DOI=10.1128/jvi.80.7.3157-3166.2006;
RA Rodriguez I., Redrejo-Rodriguez M., Rodriguez J.M., Alejo A., Salas J.,
RA Salas M.L.;
RT "African swine fever virus pB119L protein is a flavin adenine dinucleotide-
RT linked sulfhydryl oxidase.";
RL J. Virol. 80:3157-3166(2006).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA Alejo A., Matamoros T., Guerra M., Andres G.;
RT "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL J. Virol. 92:0-0(2018).
RN [5]
RP INDUCTION.
RX PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA Dixon L., Werner F.;
RT "The African Swine Fever Virus Transcriptome.";
RL J. Virol. 94:0-0(2020).
RN [6] {ECO:0007744|PDB:3GWL}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-103 IN COMPLEX WITH FAD, AND
RP SUBUNIT.
RX PubMed=19576902; DOI=10.1016/j.jmb.2009.06.070;
RA Hakim M., Fass D.;
RT "Dimer interface migration in a viral sulfhydryl oxidase.";
RL J. Mol. Biol. 391:758-768(2009).
CC -!- FUNCTION: FAD-dependent sulfhydryl oxidase that catalyzes the formation
CC of disulfide bonds in viral proteins produced in the cell cytoplasm (By
CC similarity) (PubMed:16537584). Involved in virion maturation
CC (PubMed:16537584). {ECO:0000255|PROSITE-ProRule:PRU00654,
CC ECO:0000269|PubMed:16537584}.
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:0000269|PubMed:16537584};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00654};
CC -!- SUBUNIT: Interacts with A151R. {ECO:0000269|PubMed:16537584,
CC ECO:0000269|PubMed:19576902}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:16537584}.
CC Virion {ECO:0000269|PubMed:30185597}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:32075923}.
CC -!- SIMILARITY: Belongs to the asfivirus B119L family. {ECO:0000305}.
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DR EMBL; U18466; AAA65303.1; -; Genomic_DNA.
DR RefSeq; NP_042767.1; NC_001659.2.
DR PDB; 3GWL; X-ray; 2.10 A; A/B=1-103.
DR PDBsum; 3GWL; -.
DR SMR; Q65163; -.
DR GeneID; 22220303; -.
DR KEGG; vg:22220303; -.
DR BRENDA; 1.8.3.2; 176.
DR EvolutionaryTrace; Q65163; -.
DR Proteomes; UP000000624; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; IEA:InterPro.
DR Gene3D; 1.20.120.310; -; 1.
DR InterPro; IPR039799; ALR/ERV.
DR InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR PANTHER; PTHR12645; PTHR12645; 1.
DR Pfam; PF04777; Evr1_Alr; 1.
DR SUPFAM; SSF69000; SSF69000; 1.
DR PROSITE; PS51324; ERV_ALR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; FAD; Flavoprotein; Host cytoplasm;
KW Late protein; Oxidoreductase; Reference proteome; Virion; Virulence.
FT CHAIN 1..119
FT /note="FAD-linked sulfhydryl oxidase"
FT /id="PRO_0000208551"
FT DOMAIN 1..97
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 44..47
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT HELIX 1..18
FT /evidence="ECO:0007829|PDB:3GWL"
FT HELIX 25..41
FT /evidence="ECO:0007829|PDB:3GWL"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:3GWL"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:3GWL"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:3GWL"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:3GWL"
SQ SEQUENCE 119 AA; 14378 MW; A1EE2F073ABF9726 CRC64;
MLHWGPKYWR SLHLYAIFFS DAPSWKEKYE AIQWILNFIE SLPCTRCQHH AFSYLTKNPL
TLNNSEDFQY WTFAFHNNVN NRLNKKIISW SEYKNIYEQS ILKTIEYGKT DFIGAWSSL
