ID   Y1332_PROM5             Reviewed;         221 AA.
AC   A2BXM8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=PKHD-type hydroxylase P9515_13321 {ECO:0000255|HAMAP-Rule:MF_00657};
DE            EC=1.14.11.- {ECO:0000255|HAMAP-Rule:MF_00657};
GN   OrderedLocusNames=P9515_13321;
OS   Prochlorococcus marinus (strain MIT 9515).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167542;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9515;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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=ABM72539.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000552; ABM72539.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041710633.1; NC_008817.1.
DR   AlphaFoldDB; A2BXM8; -.
DR   SMR; A2BXM8; -.
DR   STRING; 167542.P9515_13321; -.
DR   PRIDE; A2BXM8; -.
DR   EnsemblBacteria; ABM72539; ABM72539; P9515_13321.
DR   KEGG; pmc:P9515_13321; -.
DR   eggNOG; COG3128; Bacteria.
DR   HOGENOM; CLU_106663_0_0_3; -.
DR   OrthoDB; 1139586at2; -.
DR   Proteomes; UP000001589; 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..221
FT                   /note="PKHD-type hydroxylase P9515_13321"
FT                   /id="PRO_0000346506"
FT   DOMAIN          80..174
FT                   /note="Fe2OG dioxygenase"
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         100
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         155
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         165
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
SQ   SEQUENCE   221 AA;  25242 MW;  D629E1B7C3BC1048 CRC64;
     MNFLTYKLLN LEELKILKLN LNKQNELWES GKMTAGSQAS KVKENLQLNR NSEISKKYSQ
     LIRKKIITNP LIKSFALPKT IHGIMFTKSL QNMHYGRHID NPFMSSGRSD LSFTISLTNK
     ADYQGGELVI ETLNSEKKLK LDAGEIIIYP STYLHSVKKV KNGERLVCVG WIESYVKSIE
     EREYLFDLDA GAKGLLAKYG RSDELDNIFK SYSNLLRLLG N