ID A0A2U2CBY0_9RHOB Unreviewed; 218 AA.
AC A0A2U2CBY0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Peroxidase {ECO:0000313|EMBL:PWE29408.1};
GN ORFNames=DDZ14_17280 {ECO:0000313|EMBL:PWE29408.1};
OS Maritimibacter sp. 55A14.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=2174844 {ECO:0000313|EMBL:PWE29408.1, ECO:0000313|Proteomes:UP000245064};
RN [1] {ECO:0000313|EMBL:PWE29408.1, ECO:0000313|Proteomes:UP000245064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55A14 {ECO:0000313|EMBL:PWE29408.1,
RC ECO:0000313|Proteomes:UP000245064};
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Rusch D., Podicherti R., Tsui H.-C.T.,
RA Winkler M.E.;
RL Submitted (MAY-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:PWE29408.1}.
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DR EMBL; QEYE01000027; PWE29408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2CBY0; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000245064; 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:PWE29408.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245064}.
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; 24030 MW; C6C88EA6B6A66054 CRC64;
MGLRINDTAP DFTAETTEGK ISFHDWIGDG YAILFSHPKD FTPVCTTELG AMAGMIDEFA
KRNAKIIGIS VDPVDDHKRW KSDIKAVTGN DVSYPLIGDP NLEVAKLYDM LPAGEGGTSE
GRTPADNATV RTVFIIGPDK KVKLALTYPM TTGRNFDEIL RALDSIRLTA EHQVATPANW
KRGEDVIITP AVSNEDAKQR FGEYETVLPY LRKTKMPT
//