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Database: UniProt
Entry: A0A1X9YC03_9SPHN
LinkDB: A0A1X9YC03_9SPHN
Original site: A0A1X9YC03_9SPHN 
ID   A0A1X9YC03_9SPHN        Unreviewed;       181 AA.
AC   A0A1X9YC03;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Alkyl hydroperoxide reductase C {ECO:0000256|ARBA:ARBA00017462};
DE            EC=1.11.1.26 {ECO:0000256|ARBA:ARBA00013021};
DE   AltName: Full=Peroxiredoxin {ECO:0000256|ARBA:ARBA00032077};
GN   ORFNames=KC8_03185 {ECO:0000313|EMBL:ARS26294.1};
OS   Sphingomonas sp. KC8.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1030157 {ECO:0000313|EMBL:ARS26294.1, ECO:0000313|Proteomes:UP000194475};
RN   [1] {ECO:0000313|EMBL:ARS26294.1, ECO:0000313|Proteomes:UP000194475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KC8 {ECO:0000313|EMBL:ARS26294.1};
RA   Chen Y.-L., Yu C.-P., Hu A., Lee T.-H., Yang F.-C., Ismail W., Wang P.-H.,
RA   Wang C.-H., Goh K.-S., Shih C.-J., Chiang Y.-R.;
RT   "Bacteria use an extradiol dioxygenase-mediated pathway to degrade natural
RT   estrogens in aquatic ecosystems.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a hydroperoxide + H(+) + NADH = an alcohol + H2O + NAD(+);
CC         Xref=Rhea:RHEA:62628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.11.1.26;
CC         Evidence={ECO:0000256|ARBA:ARBA00000318};
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DR   EMBL; CP016306; ARS26294.1; -; Genomic_DNA.
DR   RefSeq; WP_010125068.1; NZ_CP016306.1.
DR   AlphaFoldDB; A0A1X9YC03; -.
DR   STRING; 1030157.GCA_000214335_02434; -.
DR   KEGG; spkc:KC8_03185; -.
DR   eggNOG; COG0450; Bacteria.
DR   OrthoDB; 9812811at2; -.
DR   Proteomes; UP000194475; Chromosome.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd03015; PRX_Typ2cys; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681:SF121; ALKYL HYDROPEROXIDE REDUCTASE C; 1.
DR   PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 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   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194475}.
FT   DOMAIN          3..162
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        52
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   181 AA;  19821 MW;  C947F61159FDB60A CRC64;
     MALTVGDKFP GITVPVQQGV AALPAGETID LSKTDGKWKV VFFWPKDFTF ICPTEIIGYG
     ELVKDLADRD AVLIGASTDT DFVHFAWRKS DERLANCDFP WIADNKKELA NALGIVHEDA
     GVALRATFIV DPHNVIQHVT VNGLNQGRNP AEAIRVLDAL QTDELCPCNW HQGEDVLKPA
     A
//
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