ID A0A1M6P5A0_9BACT Unreviewed; 230 AA.
AC A0A1M6P5A0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=PKHD-type hydroxylase {ECO:0000313|EMBL:SHK03072.1};
GN ORFNames=SAMN02745181_3077 {ECO:0000313|EMBL:SHK03072.1};
OS Rubritalea squalenifaciens DSM 18772.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Rubritaleaceae; Rubritalea.
OX NCBI_TaxID=1123071 {ECO:0000313|EMBL:SHK03072.1, ECO:0000313|Proteomes:UP000184510};
RN [1] {ECO:0000313|EMBL:SHK03072.1, ECO:0000313|Proteomes:UP000184510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18772 {ECO:0000313|EMBL:SHK03072.1,
RC ECO:0000313|Proteomes:UP000184510};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; FQYR01000005; SHK03072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6P5A0; -.
DR STRING; 1123071.SAMN02745181_3077; -.
DR InParanoid; A0A1M6P5A0; -.
DR OrthoDB; 9812472at2; -.
DR Proteomes; UP000184510; Unassembled WGS sequence.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR Gene3D; 4.10.860.20; Rabenosyn, Rab binding domain; 1.
DR HAMAP; MF_00657; Hydroxyl_YbiX; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR041097; PKHD_C.
DR InterPro; IPR023550; PKHD_hydroxylase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR PANTHER; PTHR41536; PKHD-TYPE HYDROXYLASE YBIX; 1.
DR PANTHER; PTHR41536:SF1; PKHD-TYPE HYDROXYLASE YBIX; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF18331; PKHD_C; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
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:UP000184510};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 78..178
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 230 AA; 25280 MW; D4F58A8A54C3E49C CRC64;
MILQIPNVLT PEQVADFRKR LDTAEWIDGK ATAGGQAIKT KDNLQLDTSN PTAIELGNLI
TQALSTNPLF VSAALPLRVL PPMFNKYTGG GTFGTHVDNA IRYIPGTGQK MRTDLSATLF
FSDPDEYEGG VLTIEDTYGT QEVKLPAGHM ILYPATSLHR VTPVTSGARV SSFFWIQSMV
RDDTQRGLLF DLDCSIQRIS QELGEHAAAE QSAVQLTGIY HNLIRQWAEV
//
