ID A0A0R2IT80_9LACO Unreviewed; 168 AA.
AC A0A0R2IT80;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Thiol peroxidase, atypical 2-Cys peroxiredoxin {ECO:0000313|EMBL:KRN65143.1};
GN ORFNames=IV80_GL000500 {ECO:0000313|EMBL:KRN65143.1};
OS Pediococcus cellicola.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=319652 {ECO:0000313|EMBL:KRN65143.1, ECO:0000313|Proteomes:UP000051568};
RN [1] {ECO:0000313|EMBL:KRN65143.1, ECO:0000313|Proteomes:UP000051568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17757 {ECO:0000313|EMBL:KRN65143.1,
RC ECO:0000313|Proteomes:UP000051568};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN65143.1}.
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DR EMBL; JQBR01000012; KRN65143.1; -; Genomic_DNA.
DR RefSeq; WP_057752585.1; NZ_JQBR01000012.1.
DR AlphaFoldDB; A0A0R2IT80; -.
DR STRING; 319652.IV80_GL000500; -.
DR PATRIC; fig|319652.3.peg.504; -.
DR OrthoDB; 9781543at2; -.
DR Proteomes; UP000051568; Unassembled WGS sequence.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR CDD; cd03014; PRX_Atyp2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR002065; TPX.
DR PANTHER; PTHR43110; THIOL PEROXIDASE; 1.
DR PANTHER; PTHR43110:SF1; THIOL PEROXIDASE; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022559,
KW ECO:0000313|EMBL:KRN65143.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:KRN65143.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000051568}.
FT DOMAIN 17..165
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 168 AA; 18888 MW; 4222F2011E14D8CC CRC64;
MDVLSNGEKV ALVGNPPEVG EQLPKFKLFN AENQKIKTKD FIGKPTLIST VPDLNTPVCK
IETKKFNQQA DHYPSVRFIT VSNNTIAEQK AWCAAEGVSN LEILSDEELS LGYEMKLYIP
NEGFLARTIF VIDAEGKIVY RQIVPEIHDE PNYLEALEVV KKYATDID
//
