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 25-MAY-2022, entry version 134.
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 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;
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 / 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=[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 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}.
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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; 746128.CADAFUBP00009334; -.
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; HVPEYIQ; -.
DR OrthoDB; 1281610at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; 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 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;
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
