ID   Y5129_PSEA7             Reviewed;         226 AA.
AC   A6VBN0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=PKHD-type hydroxylase PSPA7_5129 {ECO:0000255|HAMAP-Rule:MF_00657};
DE            EC=1.14.11.- {ECO:0000255|HAMAP-Rule:MF_00657};
GN   OrderedLocusNames=PSPA7_5129;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00657};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00657};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00657};
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABR84968.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000744; ABR84968.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_034081372.1; NC_009656.1.
DR   AlphaFoldDB; A6VBN0; -.
DR   SMR; A6VBN0; -.
DR   EnsemblBacteria; ABR84968; ABR84968; PSPA7_5129.
DR   KEGG; pap:PSPA7_5129; -.
DR   HOGENOM; CLU_106663_0_0_6; -.
DR   OrthoDB; 1139586at2; -.
DR   Proteomes; UP000001582; Chromosome.
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   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; PTHR41536; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   Pfam; PF18331; PKHD_C; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Vitamin C.
FT   CHAIN           1..226
FT                   /note="PKHD-type hydroxylase PSPA7_5129"
FT                   /id="PRO_0000346509"
FT   DOMAIN          78..178
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         96
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         98
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         159
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         169
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
SQ   SEQUENCE   226 AA;  25601 MW;  69F8F5A868B597D1 CRC64;
     MLLHIPALFT ADEVSRIRAA LEQAEWADGK ATAGYQSAKA KHNLQLPQDH PLAREIGEAM
     LQRLWNHPLF MSAALPLKVF PPLFNCYTGG GSFDFHIDNA VRDIQGGRER VRTDLSSTLF
     FSDPQDYDGG ELVIQDTYGL HQVKLPAGDL VLYPGTSLHK VNPVTRGARY ASFFWTQSLV
     REDSQRTLLF EMDQSIQQLT RDVPEHPSLI RLTGTYHNLL RRWSEL