ID A0A063BJY1_9BURK Unreviewed; 218 AA.
AC A0A063BJY1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Peroxidase {ECO:0000313|EMBL:KDB09742.1};
DE EC=1.11.1.7 {ECO:0000313|EMBL:KDB09742.1};
GN ORFNames=LIG30_0062 {ECO:0000313|EMBL:KDB09742.1};
OS Burkholderia sp. lig30.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1192124 {ECO:0000313|EMBL:KDB09742.1, ECO:0000313|Proteomes:UP000027020};
RN [1] {ECO:0000313|EMBL:KDB09742.1, ECO:0000313|Proteomes:UP000027020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LIG30 {ECO:0000313|Proteomes:UP000027020};
RA Woo H.L., Utturkar S.M., Klingeman D.M., Simmons B.A., DeAngelis K.M.,
RA Brown S.D., Hazen T.C.;
RT "Draft Genome of the Lignin-degrading Burkholderia sp. Strain LIG30,
RT Isolated from Wet Tropical Forest Soil.";
RL Submitted (MAR-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:KDB09742.1}.
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DR EMBL; JGVW01000052; KDB09742.1; -; Genomic_DNA.
DR RefSeq; WP_038710135.1; NZ_JGVW01000052.1.
DR AlphaFoldDB; A0A063BJY1; -.
DR STRING; 1192124.LIG30_0062; -.
DR PATRIC; fig|1192124.4.peg.1011; -.
DR eggNOG; COG0450; Bacteria.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000027020; 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:KDB09742.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:KDB09742.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027020}.
FT DOMAIN 3..167
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; 24361 MW; 24EFC10A1A75AA05 CRC64;
MSIRLGEEAP DFTAETTEGT IRFHEWIGDH WAILFSHPKD FTPVCTTELG YMAGLKPEFD
KRNTKIIGLS IDPVSDHQKW VKDIEETQGH AINYPLIGDA DLNVAKLYDM IHPNASGGGP
RTAVDNATVR SVFLIGPDKK VKAMLVYPMS AGRNFDEVLR LLDALQLNAK HTVATPVNWK
PGDDVIIPTS VSDDDAKQKY PQGFKTLKPY LRYVTQPR
//
