ID A0A327LR88_9RHOB Unreviewed; 217 AA.
AC A0A327LR88;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Peroxidase {ECO:0000313|EMBL:RAI52744.1};
GN ORFNames=DOO74_16480 {ECO:0000313|EMBL:RAI52744.1};
OS Rhodobacteraceae bacterium AsT-22.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2230886 {ECO:0000313|EMBL:RAI52744.1, ECO:0000313|Proteomes:UP000249713};
RN [1] {ECO:0000313|EMBL:RAI52744.1, ECO:0000313|Proteomes:UP000249713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AsT-22 {ECO:0000313|EMBL:RAI52744.1,
RC ECO:0000313|Proteomes:UP000249713};
RA Zhirakovskaya E.;
RL Submitted (JUN-2018) 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:RAI52744.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QLIW01000010; RAI52744.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327LR88; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000249713; 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:RAI52744.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000249713}.
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 217 AA; 23648 MW; 31E7673971818A7A CRC64;
MGLRINDTVP NFTAETDQGT ITFHDWIGNS WAILFSHPKD FTPVCTTEFG AVAQLAKEWE
KRGTKVIGLS VDGAEEHVKW KSDISGYAGA EAGFPIIADT SLEVSKAFDM LPADAYLPDG
RTAADSASVR SVFIIAPNKK VQLIMTYPMS VGRNFAEVLR ALDALQTTYE TPIATGANWV
KGQDVIVALT LSDEDAKQKF GNVDFKLPYL RTIADPS
//
