ID Q121S5_POLSJ Unreviewed; 219 AA.
AC Q121S5;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Peroxidase {ECO:0000313|EMBL:ABE46717.1};
DE EC=1.11.1.7 {ECO:0000313|EMBL:ABE46717.1};
GN OrderedLocusNames=Bpro_4841 {ECO:0000313|EMBL:ABE46717.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE46717.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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}.
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DR EMBL; CP000316; ABE46717.1; -; Genomic_DNA.
DR RefSeq; WP_011485702.1; NC_007948.1.
DR AlphaFoldDB; Q121S5; -.
DR STRING; 296591.Bpro_4841; -.
DR KEGG; pol:Bpro_4841; -.
DR eggNOG; COG0450; Bacteria.
DR HOGENOM; CLU_042529_4_2_4; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000001983; Chromosome.
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:ABE46717.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:ABE46717.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001983}.
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 219 AA; 24524 MW; 63348F194D26C451 CRC64;
MSLRINDTAP DFTAETTQGT VRFHEWIGDG WAILFSHPKD FTPVCTTELG YMAKIEPEFT
RRNCKLIGLS VDPVDNHTRW ARDIEETQGH LPKYPMIGDT DLAVAKLYNM LPAEEAGTSE
GRTAATNATV RSVFVIGPDK KIKLMMTYPM TTGRNFDEIL RVLDSMQMTA KHKVATPVNW
KHGDDVIIAG SVSDDDAKTL FPQGWKAPKP YLRIVKQPS
//
