ID M7MN40_9FLAO Unreviewed; 212 AA.
AC M7MN40;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Alkyl hydroperoxide reductase subunit C-like protein {ECO:0000313|EMBL:EMQ96491.1};
GN ORFNames=D778_01472 {ECO:0000313|EMBL:EMQ96491.1};
OS Xanthomarina gelatinilytica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Xanthomarina.
OX NCBI_TaxID=1137281 {ECO:0000313|EMBL:EMQ96491.1, ECO:0000313|Proteomes:UP000012024};
RN [1] {ECO:0000313|EMBL:EMQ96491.1, ECO:0000313|Proteomes:UP000012024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK20 {ECO:0000313|EMBL:EMQ96491.1,
RC ECO:0000313|Proteomes:UP000012024};
RA Kumar R., Khatri I., Vaidya B., Subramanian S., Pinnaka A.;
RT "Genome assembly of Formosa sp. AK20.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides. {ECO:0000256|ARBA:ARBA00037420}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
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:EMQ96491.1}.
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DR EMBL; ANLA01000003; EMQ96491.1; -; Genomic_DNA.
DR RefSeq; WP_007646646.1; NZ_ANLA01000003.1.
DR AlphaFoldDB; M7MN40; -.
DR PATRIC; fig|1137281.3.peg.108; -.
DR eggNOG; COG0450; Bacteria.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000012024; Unassembled WGS sequence.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR CDD; cd03015; PRX_Typ2cys; 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; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR PANTHER; PTHR10681:SF128; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE, MITOCHONDRIAL; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000012024}.
FT DOMAIN 2..179
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 51
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 212 AA; 23826 MW; E7C621BBDCD9D8C1 CRC64;
MAFVGKKFPN LNVDAMNDMG DTFKVNVLEE AVNNKKKVVL FWYPKDFTFV CPTELHAFQE
AMEEFKKRNT IVIGASCDTP EVHFAWLNTP KDNGGIEGVT YPILADSNRN LSSILGILDI
TNEKYDEETG IVTVEGDNVT YRATYLIDEE GTVFHEGINH MPLGRNVKEY LRLIDAYTHV
QEKGEVCPAN WEEGKDAMQP NAKGTAAYLA TH
//
