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Database: UniProt
Entry: A0A0W1GJA5_9SPHN
LinkDB: A0A0W1GJA5_9SPHN
Original site: A0A0W1GJA5_9SPHN 
ID   A0A0W1GJA5_9SPHN        Unreviewed;       360 AA.
AC   A0A0W1GJA5;
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:KTE54899.1};
GN   ORFNames=ATE69_08435 {ECO:0000313|EMBL:KTE54899.1};
OS   Sphingopyxis sp. H071.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1759078 {ECO:0000313|EMBL:KTE54899.1, ECO:0000313|Proteomes:UP000054127};
RN   [1] {ECO:0000313|EMBL:KTE54899.1, ECO:0000313|Proteomes:UP000054127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H071 {ECO:0000313|EMBL:KTE54899.1,
RC   ECO:0000313|Proteomes:UP000054127};
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:KTE54899.1}.
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DR   EMBL; LNSF01000004; KTE54899.1; -; Genomic_DNA.
DR   RefSeq; WP_058454789.1; NZ_LNSF01000004.1.
DR   AlphaFoldDB; A0A0W1GJA5; -.
DR   OrthoDB; 255432at2; -.
DR   Proteomes; UP000054127; 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; 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          240..337
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   360 AA;  39928 MW;  D0F0A6FD790CF9B7 CRC64;
     MSIPKPAFGV PAPWFKAPVL DGNPRYSFHT IAGRVAILFF MGSARDAGIK SALDSLLASD
     RYEGSRVCLF TVTHDAGDVS SGRIASGQYG VRHFLDYDRA ISTTYGACRE GSDRYEAYIV
     VLDRQLRVAG RYPPSQAIEA LALADRLVDE EQPDDWAPVL RIPRVLDRAT CRHLIDLYEA
     DGGEDSGFMR EVEGKTVSII DHGHKRRSDY TIADMELRRS LVGRINDCVR PAVNLAYNFD
     ATRMERYIVA CYDASVGGHF RPHRDNTTKG TAHRRFAVTI NLNDEFDGGE LRFPEFGSRT
     YRAPPGGAIV FGCGLLHEAT PVTRGRRYAF LPFLYDDDAA AQREANNVYL GEGVGAYRAG
//
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