ID A0A1Q3K7B9_9SPHI Unreviewed; 212 AA.
AC A0A1Q3K7B9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Peroxidase {ECO:0000313|EMBL:OJU28926.1};
GN ORFNames=BGN92_05880 {ECO:0000313|EMBL:OJU28926.1};
OS Sphingobacteriales bacterium 41-5.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895836 {ECO:0000313|EMBL:OJU28926.1, ECO:0000313|Proteomes:UP000187304};
RN [1] {ECO:0000313|EMBL:OJU28926.1, ECO:0000313|Proteomes:UP000187304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=41-5 {ECO:0000313|EMBL:OJU28926.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJU28926.1}.
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DR EMBL; MKRO01000023; OJU28926.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3K7B9; -.
DR Proteomes; UP000187304; 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:OJU28926.1}.
FT DOMAIN 3..159
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 212 AA; 23630 MW; 02854279282D5006 CRC64;
MSLRLGDIAP DFTAQSTEGE VKFHEFLGDG WGILFSHPAD YTPVCTTELG RTAQLKEEFA
KRNTKVLAVS VDPLDSHFGW RGDIDETQSC TVDFPILADP DRKIAELYDM IHPNASEKVT
VRSLFIIGPD KKVKLIITYP ASTGRNFHEV LRVLDSLQLT AYHSVATPAD WNAGEDVIVV
PSISTEDAIK KFPKGVKEVK PYLRYTPQPN LN
//
