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 08-NOV-2023, entry version 93. 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; African swine fever virus. 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; Evidence={ECO:0000255|PROSITE- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; Segment. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. 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 InterPro; IPR039799; ALR/ERV. DR InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf. DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase. DR PANTHER; PTHR12645; ALR/ERV; 1. DR PANTHER; PTHR12645:SF0; FAD-LINKED SULFHYDRYL OXIDASE ALR; 1. DR Pfam; PF04777; Evr1_Alr; 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; 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 //