ID K0KT29_WICCF Unreviewed; 253 AA.
AC K0KT29;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Mitochondrial peroxiredoxin PRX1 {ECO:0000313|EMBL:CCH45197.1};
DE EC=1.11.1.15 {ECO:0000313|EMBL:CCH45197.1};
GN ORFNames=BN7_4778 {ECO:0000313|EMBL:CCH45197.1};
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH45197.1, ECO:0000313|Proteomes:UP000009328};
RN [1] {ECO:0000313|EMBL:CCH45197.1, ECO:0000313|Proteomes:UP000009328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX PubMed=23193139; DOI=10.1128/EC.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA Tauch A., Kohler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCH45197.1}.
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DR EMBL; CAIF01000184; CCH45197.1; -; Genomic_DNA.
DR AlphaFoldDB; K0KT29; -.
DR STRING; 1206466.K0KT29; -.
DR eggNOG; KOG0854; Eukaryota.
DR HOGENOM; CLU_042529_4_2_1; -.
DR InParanoid; K0KT29; -.
DR Proteomes; UP000009328; 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:UP000009328}.
FT DOMAIN 42..205
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 84
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 253 AA; 28415 MW; 92CF6F4481FEFC14 CRC64;
MFTRSILRTT ASVARTTRVA PRATPIFTRG VRTFKQEDQP RLRIGSVAPN FKTQTTQGPI
DFHEYVGDSW VVFFSHPADF TPVCTTELGA FAALQEEFTK RNTKLIGLSA EGLESHNAWV
KDIEEVSKLD KFSFPIIADT DKEVSFLYDM VDEEGFKNLN GGIVQTIRSV YVIDPSKKIR
ISFTYPPSVG RNSAEVLRVI DALQLTEKRG VVTPIDWTEG KDVIIPPSVT DEAAKEKFGD
FTKVKPYLRF TKA
//
