ID Q0CMW8_ASPTN Unreviewed; 264 AA.
AC Q0CMW8;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=Mitochondrial peroxiredoxin PRX1 {ECO:0000313|EMBL:EAU34035.1};
GN ORFNames=ATEG_04966 {ECO:0000313|EMBL:EAU34035.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU34035.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. {ECO:0000256|PIRNR:PIRNR000239}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000256|ARBA:ARBA00025719}.
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DR EMBL; CH476600; EAU34035.1; -; Genomic_DNA.
DR RefSeq; XP_001214144.1; XM_001214144.1.
DR AlphaFoldDB; Q0CMW8; -.
DR STRING; 341663.Q0CMW8; -.
DR PeroxiBase; 4958; Ate1CysPrx.
DR EnsemblFungi; EAU34035; EAU34035; ATEG_04966.
DR GeneID; 4320631; -.
DR VEuPathDB; FungiDB:ATEG_04966; -.
DR eggNOG; KOG0854; Eukaryota.
DR HOGENOM; CLU_042529_4_2_1; -.
DR OMA; RLTMLYP; -.
DR OrthoDB; 103042at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR CDD; cd03016; PRX_1cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR045020; PRX_1cys.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR43503; MCG48959-RELATED; 1.
DR PANTHER; PTHR43503:SF9; PEROXIREDOXIN PRX1, MITOCHONDRIAL; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862, ECO:0000256|PIRNR:PIRNR000239};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000239};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR000239};
KW Redox-active center {ECO:0000256|PIRNR:PIRNR000239};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963}.
FT DOMAIN 53..216
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 95
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 264 AA; 29529 MW; 467C606D4CF8B9AA CRC64;
MALFLPRTGF RALSALPRAA PVSRLSAVPP RLPRVQPLTR RFLATTPQEQ PRLRLGSTAP
NFKALTTHGE IDFHEYIGDS WAILFSHPAD FTPVCTTELG AFARMKDEFE KRGVKMIGLS
ANDLGSHDKW IQDINEVSNT NLQFPIIADA DRKVAFLYDM ISQEDLDNLP EKGIAFTIRS
VFIIDPSKKI RLTMLYPAST GRNSAEVLRV IDSLQTADKK GIATPIDWNV GDDVIVPPTV
STEDAKKKFG DVRVVKPYLR YTKF
//
