(data stored in ACNUC7421 zone)

SWISSPROT: PRX5_ASPFU

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   11-DEC-2019, entry version 123.
DE   RecName: Full=Peroxiredoxin Asp f3 {ECO:0000305};
DE            Short=Prx;
DE            EC=1.11.1.15 {ECO:0000269|PubMed:27624005};
DE   AltName: Full=Thioredoxin peroxidase;
DE            Short=TPx;
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   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
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 / Af293 / CBS 101355 / FGSC A1100;
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=[protein]-dithiol + a hydroperoxide = [protein]-disulfide + an
CC         alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.15;
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 sec(-
CC         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 oxigen
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}.
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   SMR; O43099; -.
DR   STRING; 746128.CADAFUBP00009334; -.
DR   Allergome; 3121; Asp f 3.0101.
DR   Allergome; 73; Asp f 3.
DR   SwissPalm; O43099; -.
DR   PRIDE; O43099; -.
DR   EnsemblFungi; EAL85811; EAL85811; AFUA_6G02280.
DR   GeneID; 3505266; -.
DR   KEGG; afm:AFUA_6G02280; -.
DR   EuPathDB; FungiDB:Afu6g02280; -.
DR   HOGENOM; HOG000255884; -.
DR   InParanoid; O43099; -.
DR   KO; K14171; -.
DR   OMA; ARHVPEY; -.
DR   OrthoDB; 1281610at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0005623; C:cell; IEA:GOC.
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; -; 1.
DR   InterPro; IPR037944; PRX5-like.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10430; PTHR10430; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O43099.
DR   SWISS-2DPAGE; O43099.
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:0000244|PDB:5J9C"
FT   HELIX           23..25
FT                   /evidence="ECO:0000244|PDB:5J9C"
FT   STRAND          35..38
FT                   /evidence="ECO:0000244|PDB:5J9C"
FT   HELIX           39..42
FT                   /evidence="ECO:0000244|PDB:5J9C"
FT   TURN            43..45
FT                   /evidence="ECO:0000244|PDB:5J9C"
FT   STRAND          46..52
FT                   /evidence="ECO:0000244|PDB:5J9C"
FT   HELIX           59..63
FT                   /evidence="ECO:0000244|PDB:5J9C"
FT   HELIX           65..78
FT                   /evidence="ECO:0000244|PDB:5J9C"
FT   STRAND          83..90
FT                   /evidence="ECO:0000244|PDB:5J9C"
FT   HELIX           92..101
FT                   /evidence="ECO:0000244|PDB:5J9C"
FT   STRAND          108..113
FT                   /evidence="ECO:0000244|PDB:5J9C"
FT   HELIX           115..117
FT                   /evidence="ECO:0000244|PDB:5J9C"
FT   HELIX           118..122
FT                   /evidence="ECO:0000244|PDB:5J9C"
FT   STRAND          134..140
FT                   /evidence="ECO:0000244|PDB:5J9C"
FT   STRAND          143..149
FT                   /evidence="ECO:0000244|PDB:5J9C"
FT   HELIX           161..165
FT                   /evidence="ECO:0000244|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
//

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