ID A0A1T1BQX2_9FLAO Unreviewed; 212 AA.
AC A0A1T1BQX2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Peroxidase {ECO:0000313|EMBL:OOV18733.1};
GN ORFNames=BXU10_03330 {ECO:0000313|EMBL:OOV18733.1};
OS Flavobacterium sp. LM4.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1938609 {ECO:0000313|EMBL:OOV18733.1, ECO:0000313|Proteomes:UP000190722};
RN [1] {ECO:0000313|EMBL:OOV18733.1, ECO:0000313|Proteomes:UP000190722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM4 {ECO:0000313|EMBL:OOV18733.1,
RC ECO:0000313|Proteomes:UP000190722};
RA Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (JAN-2017) 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:OOV18733.1}.
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DR EMBL; MUFW01000001; OOV18733.1; -; Genomic_DNA.
DR RefSeq; WP_031456141.1; NZ_MUFW01000001.1.
DR AlphaFoldDB; A0A1T1BQX2; -.
DR STRING; 1938609.BXU10_03330; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000190722; 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 Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:OOV18733.1}.
FT DOMAIN 4..160
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 191..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 46
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 212 AA; 23558 MW; 17DF3D495B54ABD4 CRC64;
MSTLRLGDIA PDFQAETTQG TINFHEWLGD SWGVLFSHPA DFTPVCTTEL GTVANYVPEF
TKRNTKVIAL SVDGLQSHLE WIKDINETQN TTVNFPIIAD EDKKVANLYD MLHPNASDKF
TVRSVFVIGS DKKIKLTLTY PASTGRNFDE LLRVIDSLQL TANYSVATPA NWKDGQDVVI
SPAVPDSDIP AKFPKGHTPI KPYLRLTPQP NK
//
