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Database: UniProt
Entry: W0BC86_9GAMM
LinkDB: W0BC86_9GAMM
Original site: W0BC86_9GAMM 
ID   W0BC86_9GAMM            Unreviewed;       205 AA.
AC   W0BC86;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Putative proline hydroxylase {ECO:0000313|EMBL:AHE66034.1};
GN   ORFNames=Loa_00457 {ECO:0000313|EMBL:AHE66034.1};
OS   Legionella oakridgensis ATCC 33761 = DSM 21215.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1268635 {ECO:0000313|EMBL:AHE66034.1, ECO:0000313|Proteomes:UP000018838};
RN   [1] {ECO:0000313|EMBL:AHE66034.1, ECO:0000313|Proteomes:UP000018838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OR-10, ATCC 33761 {ECO:0000313|Proteomes:UP000018838};
RX   PubMed=23932911; DOI=10.1016/j.ijmm.2013.07.003;
RA   Brzuszkiewicz E., Schulz T., Rydzewski K., Daniel R., Gillmaier N.,
RA   Dittmann C., Holland G., Schunder E., Lautner M., Eisenreich W., Luck C.,
RA   Heuner K.;
RT   "Legionella oakridgensis ATCC 33761 genome sequence and phenotypic
RT   characterization reveals its replication capacity in amoebae.";
RL   Int. J. Med. Microbiol. 303:514-528(2013).
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR   EMBL; CP004006; AHE66034.1; -; Genomic_DNA.
DR   RefSeq; WP_025384929.1; NZ_CP004006.1.
DR   AlphaFoldDB; W0BC86; -.
DR   STRING; 1268635.Loa_00457; -.
DR   KEGG; lok:Loa_00457; -.
DR   PATRIC; fig|1268635.3.peg.448; -.
DR   eggNOG; COG3751; Bacteria.
DR   HOGENOM; CLU_022206_1_0_6; -.
DR   Proteomes; UP000018838; Chromosome.
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; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR   PANTHER; PTHR12907; EGL NINE HOMOLOG-RELATED; 1.
DR   PANTHER; PTHR12907:SF26; HIF PROLYL HYDROXYLASE, ISOFORM C; 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:UP000018838};
KW   Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT   DOMAIN          91..198
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   205 AA;  24075 MW;  E9D3D2457FE562E4 CRC64;
     MIQLENIEDK IHQHGFHIID NFLNDFHYQT LHILIKTKHQ DGHFRDAKIG HGQQAVHNNK
     IRTDKLCWLS KDSEHDALQV YFAAVNNISQ RLNQALFLGL VDFESHFAVY NPGSFYKKHV
     DQFATTRDRR ISCVYYLNKT WKAGDGGELI LYDCDQDNRD LVTIQPIPNR FVCFRSEFPH
     EVNTTYQMRY SLVGWLKSRA LNAFT
//
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