PRX5_EMENI
ID PRX5_EMENI Reviewed; 168 AA.
AC Q5ASN8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Putative peroxiredoxin prxA {ECO:0000305};
DE Short=Prx;
DE EC=1.11.1.24 {ECO:0000269|PubMed:17631497};
DE AltName: Full=Thioredoxin peroxidase;
DE Short=TPx;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000305};
GN Name=prxA {ECO:0000303|PubMed:19965775};
GN Synonyms=PRX5 {ECO:0000303|PubMed:17631497}; ORFNames=AN8692;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17258477; DOI=10.1016/j.fgb.2006.12.001;
RA Kim Y., Nandakumar M.P., Marten M.R.;
RT "Proteome map of Aspergillus nidulans during osmoadaptation.";
RL Fungal Genet. Biol. 44:886-895(2007).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP INTERACTION WITH TRXA.
RX PubMed=17631497; DOI=10.1074/jbc.m704298200;
RA Thoen M., Al-Abdallah Q., Hortschansky P., Brakhage A.A.;
RT "The thioredoxin system of the filamentous fungus Aspergillus nidulans:
RT impact on development and oxidative stress response.";
RL J. Biol. Chem. 282:27259-27269(2007).
RN [5]
RP INDUCTION, AND ACTIVE SITE.
RX PubMed=19965775; DOI=10.1093/nar/gkp1091;
RA Thoen M., Al Abdallah Q., Hortschansky P., Scharf D.H., Eisendle M.,
RA Haas H., Brakhage A.A.;
RT "The CCAAT-binding complex coordinates the oxidative stress response in
RT eukaryotes.";
RL Nucleic Acids Res. 38:1098-1113(2010).
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 (By similarity). Involved in osmoadaptation
CC (PubMed:17258477). {ECO:0000250|UniProtKB:O43099,
CC ECO:0000250|UniProtKB:P38013, ECO:0000269|PubMed:17258477}.
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:17631497};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.3 uM for H(2)O(2) {ECO:0000269|PubMed:17631497};
CC Vmax=6.8 umol/min/mg enzyme {ECO:0000269|PubMed:17631497};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By similarity).
CC Interacts with thioredoxin trxA (PubMed:17631497).
CC {ECO:0000250|UniProtKB:P38013, ECO:0000269|PubMed:17631497}.
CC -!- INDUCTION: Down-regulated when grown with elevated levels of potassium
CC chloride (PubMed:17258477). Induced under oxidative stress conditions
CC dependent on transcription factor napA (PubMed:19965775).
CC {ECO:0000269|PubMed:17258477, ECO:0000269|PubMed:19965775}.
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:0000250|UniProtKB:P38013}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AACD01000160; EAA60241.1; -; Genomic_DNA.
DR EMBL; BN001303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_681961.1; XM_676869.1.
DR AlphaFoldDB; Q5ASN8; -.
DR SMR; Q5ASN8; -.
DR STRING; 227321.Q5ASN8; -.
DR PRIDE; Q5ASN8; -.
DR EnsemblFungi; EAA60241; EAA60241; AN8692.2.
DR GeneID; 2868548; -.
DR KEGG; ani:AN8692.2; -.
DR VEuPathDB; FungiDB:AN8692; -.
DR HOGENOM; CLU_072440_1_1_1; -.
DR InParanoid; Q5ASN8; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:AspGD.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0071470; P:cellular response to osmotic stress; IEP:AspGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEP:AspGD.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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 Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome; Stress response.
FT CHAIN 1..168
FT /note="Putative peroxiredoxin prxA"
FT /id="PRO_0000348283"
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:19965775"
FT DISULFID 31
FT /note="Interchain (with C-61); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P38013"
FT DISULFID 61
FT /note="Interchain (with C-31); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P38013"
SQ SEQUENCE 168 AA; 18527 MW; 0B2A04F2E340BB89 CRC64;
MSGLKAGDSF PADVVFSYIP WTEEKGEITS CGIPINYYAS KEWADKKVIL FALPGAFTPV
CSARHVPEYI ERLPEIRAKG VDVVAVLAYN DAFVMSAWGK ANGVKNDDIL FLSDPEAKFS
KSIGWADEEG RTKRYAIVLD HGKVTYAALE PAKNHLEFSS AETVIKHL
