ID A0A0M2Y408_9SPHI Unreviewed; 211 AA.
AC A0A0M2Y408;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Peroxidase {ECO:0000313|EMBL:KKO92609.1};
GN ORFNames=AAW12_03920 {ECO:0000313|EMBL:KKO92609.1};
OS Sphingobacterium sp. Ag1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1643451 {ECO:0000313|EMBL:KKO92609.1, ECO:0000313|Proteomes:UP000034524};
RN [1] {ECO:0000313|EMBL:KKO92609.1, ECO:0000313|Proteomes:UP000034524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKO92609.1,
RC ECO:0000313|Proteomes:UP000034524};
RA Pei D., Yu W., Kukutla P., Xu J.;
RT "Draft Genome Sequences of Sphingobacterium sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) 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:KKO92609.1}.
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DR EMBL; LBGU01000024; KKO92609.1; -; Genomic_DNA.
DR RefSeq; WP_046672310.1; NZ_LBGU01000024.1.
DR AlphaFoldDB; A0A0M2Y408; -.
DR PATRIC; fig|1643451.3.peg.3126; -.
DR Proteomes; UP000034524; 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:KKO92609.1}.
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 211 AA; 23754 MW; 8B4CABB2412F4E1C CRC64;
MSLRLGDEAP NFKAQTTIGE IDFHDYIKDS WVVFFSHPSD YTPVCTTELG RTAKLKSEFD
KRGVKAIALS VDNVNDHLNW IKDINETLNT EVNFPVIADE DHHVSELYDM IHPNASATAT
VRSVFIIGPD KKIKLTLTYP ASTGRNFDEI LRVIDSLQLT ADYQVATPAD WKHGEDVIVV
PAIKTEDIPA KFPKGFKEIK PYLRTTPQPN L
//
