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Database: UniProt
Entry: A0A0A0HH65_9RHOB
LinkDB: A0A0A0HH65_9RHOB
Original site: A0A0A0HH65_9RHOB 
ID   A0A0A0HH65_9RHOB        Unreviewed;       217 AA.
AC   A0A0A0HH65;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=1-Cys peroxiredoxin {ECO:0000313|EMBL:KGM86301.1};
DE            EC=1.11.1.15 {ECO:0000313|EMBL:KGM86301.1};
GN   ORFNames=rosmuc_03864 {ECO:0000313|EMBL:KGM86301.1};
OS   Roseovarius mucosus DSM 17069.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1288298 {ECO:0000313|EMBL:KGM86301.1, ECO:0000313|Proteomes:UP000030021};
RN   [1] {ECO:0000313|EMBL:KGM86301.1, ECO:0000313|Proteomes:UP000030021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17069 {ECO:0000313|EMBL:KGM86301.1,
RC   ECO:0000313|Proteomes:UP000030021};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (JAN-2013) 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:KGM86301.1}.
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DR   EMBL; AONH01000020; KGM86301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A0HH65; -.
DR   STRING; 215743.ROSMUCSMR3_02674; -.
DR   PATRIC; fig|1288298.3.peg.3873; -.
DR   eggNOG; COG0450; Bacteria.
DR   HOGENOM; CLU_042529_4_2_5; -.
DR   OrthoDB; 9812811at2; -.
DR   Proteomes; UP000030021; 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:KGM86301.1};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:KGM86301.1}.
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;  23451 MW;  D9AD2A578465487E CRC64;
     MGLRINDVIP DLTVETDLGT ISLHEWIGDS WAILFSHPKD FTPVCTTEFG AVARLAEEWE
     KRGCKVIGVS VDGVEDHRKW KGDIEKVAGS AAGFPIIADA GLVVSKAFDM LPAEAYLPDG
     RTPNDSATVR SVFIIGPDKQ LKLSMTYPMT VGRNFAEVLR ALDALQTSSR NGVATPADWT
     VGQDVIIPAS LSDADAEAKF GSFDKVLPYL RKTSLKG
//
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