ID A0A080LW20_9PROT Unreviewed; 218 AA.
AC A0A080LW20;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Alkyl hydroperoxide reductase subunit C {ECO:0000313|EMBL:KFB71930.1};
DE EC=1.11.1.15 {ECO:0000313|EMBL:KFB71930.1};
GN ORFNames=AW09_002909 {ECO:0000313|EMBL:KFB71930.1};
OS Candidatus Accumulibacter phosphatis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=327160 {ECO:0000313|EMBL:KFB71930.1, ECO:0000313|Proteomes:UP000020077};
RN [1] {ECO:0000313|EMBL:KFB71930.1, ECO:0000313|Proteomes:UP000020077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA-91 {ECO:0000313|Proteomes:UP000020077};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
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:KFB71930.1}.
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DR EMBL; JDVG02000465; KFB71930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A080LW20; -.
DR Proteomes; UP000020077; 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:SF4; PEROXIREDOXIN-6; 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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KFB71930.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:KFB71930.1}.
FT DOMAIN 3..168
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 45
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 218 AA; 24335 MW; BDD94CDB1B08685C CRC64;
MSLRINDVAP DFSAETTQGS IRFHEWIGDS WAILFSHPKD FTPVCTTELG YMAGIEDKFT
SRNCKLIGLS IDPVDNHARW AKDIEETQGH LPRYPMIGDT DLAVAKLYNM LPAEEPGTSE
GRTAATNATV RSVFVIGPDK KIKLMMTYPM TTGRNFDEIL RALDSMQLTA KHKVATPVNW
KQGEDVIIAG SVSDEEAKTL FPEGWKAPKP YLRIVKHP
//
