ID A0A1I1VML6_9BURK Unreviewed; 227 AA.
AC A0A1I1VML6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=PKHD-type hydroxylase {ECO:0000313|EMBL:SFD82303.1};
GN ORFNames=SAMN04489710_106317 {ECO:0000313|EMBL:SFD82303.1};
OS Paracidovorax konjaci.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Paracidovorax.
OX NCBI_TaxID=32040 {ECO:0000313|EMBL:SFD82303.1, ECO:0000313|Proteomes:UP000199517};
RN [1] {ECO:0000313|EMBL:SFD82303.1, ECO:0000313|Proteomes:UP000199517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7481 {ECO:0000313|EMBL:SFD82303.1,
RC ECO:0000313|Proteomes:UP000199517};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00657};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00657};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961,
CC ECO:0000256|HAMAP-Rule:MF_00657};
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DR EMBL; FOMQ01000006; SFD82303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1VML6; -.
DR STRING; 32040.SAMN04489710_106317; -.
DR OrthoDB; 9812472at2; -.
DR Proteomes; UP000199517; Unassembled WGS sequence.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
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, ECO:0000256|HAMAP-
KW Rule:MF_00657};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00657};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00657};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00657};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896, ECO:0000256|HAMAP-Rule:MF_00657}.
FT DOMAIN 78..178
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT BINDING 96
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00657"
FT BINDING 98
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00657"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00657"
FT BINDING 169
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00657"
SQ SEQUENCE 227 AA; 25032 MW; 3199EC73559B78E4 CRC64;
MLITIDRLLD KDEVRHFRER LDAAAWQGGA ATAGTLARAV KQNQQLEDGS PLAVELGHRI
LRALGQHPTF VSAALPRTIY PPKFNRYADG GTYGAHVDSA VMHLPGTLQP MRTDVSATLF
LAEPGEYDGG ELEIEGPFGV QSVKLEAGDL VLYPSTSLHR VTPVTRGARI ASFLWIESLV
ADEGERTLLF DLDQSIQRLT PLVEASDPRL LQLTGVYHNL LRRWART
//
