ID G8NP47_GRAMM Unreviewed; 218 AA.
AC G8NP47;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Peroxidase {ECO:0000313|EMBL:AEU38246.1};
DE EC=1.11.1.7 {ECO:0000313|EMBL:AEU38246.1};
GN OrderedLocusNames=AciX8_3963 {ECO:0000313|EMBL:AEU38246.1};
OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU38246.1, ECO:0000313|Proteomes:UP000007113};
RN [1] {ECO:0000313|EMBL:AEU38246.1, ECO:0000313|Proteomes:UP000007113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8
RC {ECO:0000313|Proteomes:UP000007113};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA Haggblom M., Woyke T.;
RT "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL Submitted (NOV-2011) 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}.
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DR EMBL; CP003130; AEU38246.1; -; Genomic_DNA.
DR RefSeq; WP_014267117.1; NC_016631.1.
DR AlphaFoldDB; G8NP47; -.
DR STRING; 682795.AciX8_3963; -.
DR KEGG; gma:AciX8_3963; -.
DR eggNOG; COG0450; Bacteria.
DR HOGENOM; CLU_042529_4_2_0; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000007113; Chromosome.
DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
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:AEU38246.1};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:AEU38246.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007113}.
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 218 AA; 23958 MW; D8DCFF3E1FCFFC97 CRC64;
MSLRINDVAP DFTAETTQGT VHFHEWIGDN WAVLFSHPKD FTPVCTTELG AVAALETQFA
QRGAKVIGLS VDPVESHGKW AQDIEDVGGH KVNYPIIGDP ELKIAKLYDM LAAEDGDSCE
GRTPANNAPV RTVFIVGPDK RIKLQIAYPM TTGRNFDEII RVLDSMQLTA KHKVATPANW
KQGEDIIITG AVSNEEADKI FPGYKTVKPY LRTAAQPK
//
