ID   A0A2R7L8K3_9CAUL        Unreviewed;       366 AA.
AC   A0A2R7L8K3;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Peroxiredoxin {ECO:0000313|EMBL:PTT06002.1};
GN   ORFNames=DBR10_13650 {ECO:0000313|EMBL:PTT06002.1};
OS   Caulobacter sp. HMWF025.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=2056860 {ECO:0000313|EMBL:PTT06002.1, ECO:0000313|Proteomes:UP000244835};
RN   [1] {ECO:0000313|Proteomes:UP000244835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMWF025 {ECO:0000313|Proteomes:UP000244835};
RA   Muscarella M.E.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
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:PTT06002.1}.
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; QAII01000130; PTT06002.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R7L8K3; -.
DR   OrthoDB; 255432at2; -.
DR   Proteomes; UP000244835; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT   DOMAIN          239..337
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   366 AA;  40743 MW;  2DAC7BD3449A4FCE CRC64;
     MRMPLLIGDS APFFRAATPT NPDYAFDSVA GRYVVLAFYP SQDMATAIAV SAAVQANRSL
     FDDDKTAFFG VLRSEAMIQG ARNSMPGVRW FLDLNRAVSH LYGMEAPDGT ELTGWLVLDP
     MLRVIAVTSL DQTAQVMALL AGLPAVDDHA ATELFAPVLV LPRVFDPDLC HRLIRAYETG
     LQEPSGFMRE VDGRTVGVFD SASKRRTDHI IEDGPVRAEI RSCITRRLLP QIQRAFSFRA
     TRMERYIVAC YDGAEGGFFR PHRDDMSKGT DHRRFAVTIN LNAEDYEGGD LIFPEFGSRT
     YRAPTGGAVV FSCSLLHGAE PVTAGRRYAF LPFLYDEAAA QLREKHAKFL EPDKADYRAI
     EQTEIR
//