GenomeNet

Database: UniProt
Entry: A0A0W1DA60_9SPHN
LinkDB: A0A0W1DA60_9SPHN
Original site: A0A0W1DA60_9SPHN 
ID   A0A0W1DA60_9SPHN        Unreviewed;       368 AA.
AC   A0A0W1DA60;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Peroxiredoxin {ECO:0000313|EMBL:KTE14968.1};
GN   ORFNames=ATE71_07635 {ECO:0000313|EMBL:KTE14968.1};
OS   Sphingopyxis sp. H115.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1759073 {ECO:0000313|EMBL:KTE14968.1, ECO:0000313|Proteomes:UP000054021};
RN   [1] {ECO:0000313|EMBL:KTE14968.1, ECO:0000313|Proteomes:UP000054021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H115 {ECO:0000313|EMBL:KTE14968.1,
RC   ECO:0000313|Proteomes:UP000054021};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) 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:KTE14968.1}.
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; LNSA01000008; KTE14968.1; -; Genomic_DNA.
DR   RefSeq; WP_058802877.1; NZ_LNSA01000008.1.
DR   AlphaFoldDB; A0A0W1DA60; -.
DR   STRING; 1759073.ATE71_07635; -.
DR   OrthoDB; 255432at2; -.
DR   Proteomes; UP000054021; Unassembled WGS sequence.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
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; IPR000866; AhpC/TSA.
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   Pfam; PF00578; AhpC-TSA; 1.
DR   SMART; SM00702; P4Hc; 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          249..346
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   368 AA;  41069 MW;  1328A62439811C4A CRC64;
     MLQSETRLDS IPKPIVGSAA PWFKAHVLDG NPQYTFHTVA GRAVLLFFMG SATGNGIEAA
     RDLLMADADR FDDSRCSFFG ITIDTDDHVA GRVKTRLPGI RYILDSDRAV SQAYGACSPD
     SDHYEPYIIV LDRQLRVAGR YHLPDAGKAL ALIDRLTREG KPEDWAPVLS VPRVFDRATC
     QRLIDLYEAE GGRDSGFMRE VDGKTVSVID HGHKRRSDVT IRDEAFCRAL SARVNHCLRP
     VIQRAFNFDA TRMERYIVAC YDASVAGHFR AHRDNTTMGT AHRRFAVTIN LNDDFDGGEL
     RFPEFGTRTY RPAPGGAIVF GCGLLHEATP VTRGRRYAFL PFLYDDEAAA QREANNQYLG
     EGVGAYRQ
//
DBGET integrated database retrieval system