ID A0A0Q6WQF3_9BURK Unreviewed; 183 AA.
AC A0A0Q6WQF3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Iron-regulated protein {ECO:0000313|EMBL:KQV93406.1};
GN ORFNames=ASC87_27260 {ECO:0000313|EMBL:KQV93406.1};
OS Rhizobacter sp. Root1221.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736433 {ECO:0000313|EMBL:KQV93406.1, ECO:0000313|Proteomes:UP000051465};
RN [1] {ECO:0000313|EMBL:KQV93406.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQV93406.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV93406.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQV93406.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
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:KQV93406.1}.
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DR EMBL; LMDI01000030; KQV93406.1; -; Genomic_DNA.
DR RefSeq; WP_056666393.1; NZ_LMDI01000030.1.
DR AlphaFoldDB; A0A0Q6WQF3; -.
DR STRING; 1736433.ASC87_27260; -.
DR OrthoDB; 269774at2; -.
DR Proteomes; UP000051465; 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 Reference proteome {ECO:0000313|Proteomes:UP000051465};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 87..178
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 183 AA; 20962 MW; D456B0ADB7C9D84E CRC64;
MNVNRLGAGV FTIEGFLTPA ECAQFIADSE TLGYEEASVR TDDGERLYKD ARNNDRIILD
RRELASSLYQ RAKPVLPAEV KGWVVSGFNE RFRYYRYEKQ QQFVWHQDGT VRISETEESL
LTFMIYLNDE FEGGSTDFGW ESVRPVQGMA LVFPHRLRHQ GSVVTGGVKY VLRTDVMYTG
NNA
//