ID PRX5_ASPFU Reviewed; 168 AA. AC O43099; Q4WCS7; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 141. DE RecName: Full=Peroxiredoxin Asp f3 {ECO:0000305}; DE Short=Prx; DE EC=1.11.1.24 {ECO:0000269|PubMed:27624005}; DE AltName: Full=Thioredoxin peroxidase; DE Short=TPx; DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000305}; DE AltName: Allergen=Asp f 3 {ECO:0000303|PubMed:10756236, ECO:0000303|PubMed:9412580}; GN Name=aspf3 {ECO:0000303|PubMed:9412580}; ORFNames=AFUA_6G02280; OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / OS Af293) (Neosartorya fumigata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=330879; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN. RC STRAIN=ATCC 42202 / AF-102 / Ag 507; RX PubMed=9412580; DOI=10.1164/ajrccm.156.6.9702087; RA Hemmann S., Blaser K., Crameri R.; RT "Allergens of Aspergillus fumigatus and Candida boidinii share IgE-binding RT epitopes."; RL Am. J. Respir. Crit. Care Med. 156:1956-1962(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293; RX PubMed=16372009; DOI=10.1038/nature04332; RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L., RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., RA Barrell B.G., Denning D.W.; RT "Genomic sequence of the pathogenic and allergenic filamentous fungus RT Aspergillus fumigatus."; RL Nature 438:1151-1156(2005). RN [3] RP PROTEIN SEQUENCE OF 2-9, AND ALLERGEN. RX PubMed=10756236; DOI=10.1067/mai.2000.105220; RA Shen H.D., Wang C.W., Chou H., Lin W.L., Tam M.F., Huang M.H., Kuo M.L., RA Wang S.R., Han S.H.; RT "Complementary DNA cloning and immunologic characterization of a new RT Penicillium citrinum allergen (Pen c 3)."; RL J. Allergy Clin. Immunol. 105:827-833(2000). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 2-168, DISULFIDE BOND, FUNCTION, RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, RP AND DISRUPTION PHENOTYPE. RX PubMed=27624005; DOI=10.1038/srep33396; RA Hillmann F., Bagramyan K., Strassburger M., Heinekamp T., Hong T.B., RA Bzymek K.P., Williams J.C., Brakhage A.A., Kalkum M.; RT "The crystal structure of peroxiredoxin Asp f3 provides mechanistic insight RT into oxidative stress resistance and virulence of Aspergillus fumigatus."; RL Sci. Rep. 6:33396-33396(2016). CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of CC hydrogen peroxide and organic hydroperoxides to water and alcohols, CC respectively. Plays a role in cell protection against oxidative stress CC by detoxifying peroxides and as sensor of hydrogen peroxide-mediated CC signaling events. Required for virulence. CC {ECO:0000269|PubMed:27624005}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]- CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA- CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, CC ChEBI:CHEBI:50058; EC=1.11.1.24; CC Evidence={ECO:0000269|PubMed:27624005}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=72.29 uM for H(2)O(2) {ECO:0000269|PubMed:27624005}; CC KM=70.48 uM for tert-butyl hydroperoxide CC {ECO:0000269|PubMed:27624005}; CC Note=kcat is 12.53 sec(-1) with H(2)O(2) as substrate and 12.96 CC sec(-1) with tert-butyl hydroperoxide as substrate. CC {ECO:0000269|PubMed:27624005}; CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. CC {ECO:0000269|PubMed:27624005}. CC -!- DISRUPTION PHENOTYPE: Renders cells sensitive to reactive oxygen CC species. Renders A.fumigatus avirulent in a mouse model of pulmonary CC aspergillosis. {ECO:0000269|PubMed:27624005}. CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE CC (PubMed:9412580, PubMed:10756236). Shares common IgE-binding epitopes CC with allergen Cand b 2 of Candida boidinii (PubMed:9412580). CC {ECO:0000269|PubMed:10756236, ECO:0000269|PubMed:9412580}. CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide CC bridge. The disulfide is subsequently reduced by an appropriate CC electron donor to complete the catalytic cycle. In this typical 2-Cys CC Prx, C(R) is provided by the other dimeric subunit to form an CC intersubunit disulfide. The disulfide is subsequently reduced by CC thioredoxin. {ECO:0000305|PubMed:27624005}. CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily. CC {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; U58050; AAB95638.1; -; mRNA. DR EMBL; AAHF01000012; EAL85811.1; -; Genomic_DNA. DR RefSeq; XP_747849.1; XM_742756.1. DR PDB; 5J9B; X-ray; 2.10 A; A/B=2-168. DR PDB; 5J9C; X-ray; 1.96 A; A/B=2-168. DR PDBsum; 5J9B; -. DR PDBsum; 5J9C; -. DR AlphaFoldDB; O43099; -. DR SMR; O43099; -. DR STRING; 330879.O43099; -. DR Allergome; 3121; Asp f 3.0101. DR Allergome; 73; Asp f 3. DR SwissPalm; O43099; -. DR EnsemblFungi; EAL85811; EAL85811; AFUA_6G02280. DR GeneID; 3505266; -. DR KEGG; afm:AFUA_6G02280; -. DR VEuPathDB; FungiDB:Afu6g02280; -. DR eggNOG; KOG0541; Eukaryota. DR HOGENOM; CLU_072440_1_1_1; -. DR InParanoid; O43099; -. DR OMA; TPSCHAN; -. DR OrthoDB; 593245at2759; -. DR Proteomes; UP000002530; Chromosome 6. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0005777; C:peroxisome; IBA:GO_Central. DR GO; GO:0019863; F:IgE binding; IDA:AspGD. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:UniProtKB. DR GO; GO:0045454; P:cell redox homeostasis; IDA:UniProtKB. DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB. DR CDD; cd03013; PRX5_like; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR037944; PRX5-like. DR InterPro; IPR013740; Redoxin. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR10430; PEROXIREDOXIN; 1. DR PANTHER; PTHR10430:SF30; PEROXIREDOXIN PRXA-RELATED; 1. DR Pfam; PF08534; Redoxin; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Allergen; Antioxidant; Direct protein sequencing; KW Disulfide bond; Oxidoreductase; Peroxidase; Redox-active center; KW Reference proteome. FT CHAIN 1..168 FT /note="Peroxiredoxin Asp f3" FT /id="PRO_0000056603" FT DOMAIN 4..158 FT /note="Thioredoxin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT ACT_SITE 61 FT /note="Cysteine sulfenic acid (-SOH) intermediate" FT /evidence="ECO:0000305|PubMed:27624005" FT DISULFID 31 FT /note="Interchain (with C-61); in linked form" FT /evidence="ECO:0000269|PubMed:27624005" FT DISULFID 61 FT /note="Interchain (with C-31); in linked form" FT /evidence="ECO:0000269|PubMed:27624005" FT STRAND 15..18 FT /evidence="ECO:0007829|PDB:5J9C" FT HELIX 23..25 FT /evidence="ECO:0007829|PDB:5J9C" FT STRAND 35..38 FT /evidence="ECO:0007829|PDB:5J9C" FT HELIX 39..42 FT /evidence="ECO:0007829|PDB:5J9C" FT TURN 43..45 FT /evidence="ECO:0007829|PDB:5J9C" FT STRAND 46..52 FT /evidence="ECO:0007829|PDB:5J9C" FT HELIX 59..63 FT /evidence="ECO:0007829|PDB:5J9C" FT HELIX 65..78 FT /evidence="ECO:0007829|PDB:5J9C" FT STRAND 83..90 FT /evidence="ECO:0007829|PDB:5J9C" FT HELIX 92..101 FT /evidence="ECO:0007829|PDB:5J9C" FT STRAND 108..113 FT /evidence="ECO:0007829|PDB:5J9C" FT HELIX 115..117 FT /evidence="ECO:0007829|PDB:5J9C" FT HELIX 118..122 FT /evidence="ECO:0007829|PDB:5J9C" FT STRAND 134..140 FT /evidence="ECO:0007829|PDB:5J9C" FT STRAND 143..149 FT /evidence="ECO:0007829|PDB:5J9C" FT HELIX 161..165 FT /evidence="ECO:0007829|PDB:5J9C" SQ SEQUENCE 168 AA; 18453 MW; AFFCD72C5A1CCBB2 CRC64; MSGLKAGDSF PSDVVFSYIP WSEDKGEITA CGIPINYNAS KEWADKKVIL FALPGAFTPV CSARHVPEYI EKLPEIRAKG VDVVAVLAYN DAYVMSAWGK ANQVTGDDIL FLSDPDARFS KSIGWADEEG RTKRYALVID HGKITYAALE PAKNHLEFSS AETVLKHL //