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Database: UniProt
Entry: J2K312_9BURK
LinkDB: J2K312_9BURK
Original site: J2K312_9BURK 
ID   J2K312_9BURK            Unreviewed;       296 AA.
AC   J2K312;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=2OG-Fe(II) oxygenase superfamily enzyme {ECO:0000313|EMBL:EJL74535.1};
GN   ORFNames=PMI12_03003 {ECO:0000313|EMBL:EJL74535.1};
OS   Variovorax sp. CF313.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1144315 {ECO:0000313|EMBL:EJL74535.1, ECO:0000313|Proteomes:UP000007277};
RN   [1] {ECO:0000313|EMBL:EJL74535.1, ECO:0000313|Proteomes:UP000007277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF313 {ECO:0000313|EMBL:EJL74535.1,
RC   ECO:0000313|Proteomes:UP000007277};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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:EJL74535.1}.
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DR   EMBL; AKIW01000053; EJL74535.1; -; Genomic_DNA.
DR   RefSeq; WP_007833755.1; NZ_AKIW01000053.1.
DR   AlphaFoldDB; J2K312; -.
DR   PATRIC; fig|1144315.3.peg.2995; -.
DR   Proteomes; UP000007277; 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; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR045054; P4HA-like.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR   PANTHER; PTHR10869:SF207; P4HA_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   SMART; SM00702; P4Hc; 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          175..284
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   296 AA;  32285 MW;  DAEC2F12D6AEE624 CRC64;
     MDAVLRFSPA LSDWVLHNLR QGCAPANVIK AMRAQDMPPE AARTIVDAFV FALRTGSPVP
     VDSVTVAPLY QYEPPRLPPG ASIRTTDRLV RVAARAAQPA MAVLDDVFDP QECEELIALA
     RPRLAPSTTV DPLSGRDLVG EQRSSLGMFF RLRENAFIAR LDQRVSELMN LPVENGEGLQ
     VLCYPAGAQS MPHFDFLVPS NAANKASLAR SGQRVSTLVS YLNEVEEGGE TIFPECGWSV
     PPRRGSAVYF EYCNSLGQVD HASLHAGGPV LHGEKWVATK WMRQRRFVAA GEASDG
//
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