ID   LYS4O_FLAJ1             Reviewed;         370 AA.
AC   A5FF23;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=L-lysine 4-hydroxylase {ECO:0000305|Ref.2};
DE            EC=1.14.11.- {ECO:0000269|Ref.2};
DE   AltName: Full=Alpha-ketoglutarate-dependent dioxygenase {ECO:0000303|Ref.2};
DE   AltName: Full=KDO3 {ECO:0000303|Ref.2};
DE   AltName: Full=L-lysine hydroxylase {ECO:0000303|Ref.2};
GN   OrderedLocusNames=Fjoh_3169 {ECO:0000312|EMBL:ABQ06186.1};
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX   PubMed=19717629; DOI=10.1128/aem.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOTECHNOLOGY.
RX   DOI=10.1002/cctc.201402498;
RA   Baud D., Saaidi P.-L., Monfleur A., Harari M., Cuccaro J., Fossey A.,
RA   Besnard M., Debard A., Mariage A., Pellouin V., Petit J.-L., Salanoubat M.,
RA   Weissenbach J., de Berardinis V., Zaparucha A.;
RT   "Synthesis of mono- and dihydroxylated amino acids with new alpha-
RT   ketoglutarate-dependent dioxygenases: biocatalytic oxidation of C-H
RT   bonds.";
RL   ChemCatChem 6:3012-3017(2014).
CC   -!- FUNCTION: Alpha-ketoglutarate-dependent dioxygenase that in vitro
CC       catalyzes the regio- and stereoselective hydroxylation of L-lysine,
CC       leading to (4R)-4-hydroxy-L-lysine. To a lesser extent, can also use
CC       (3S)-3-hydroxy-L-lysine as substrate, producing the dihydroxylated
CC       product (3R,4R)-3,4-hydroxy-L-lysine. Cannot use D-lysine or L-
CC       ornithine as substrate. {ECO:0000269|Ref.2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-lysine + O2 = (4R)-4-hydroxy-L-lysine + CO2
CC         + succinate; Xref=Rhea:RHEA:42420, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:32551, ChEBI:CHEBI:77410; Evidence={ECO:0000269|Ref.2};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z4Z5};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9Z4Z5};
CC   -!- BIOTECHNOLOGY: Being totally regio- and stereoselective, this enzyme is
CC       of interest for biocatalytic purposes to produce chiral scaffolds that
CC       are of synthetic value in the preparation of more complex
CC       functionalized chiral molecules such as natural products and analogs.
CC       {ECO:0000305|Ref.2}.
CC   -!- SIMILARITY: Belongs to the clavaminate synthase family. {ECO:0000305}.
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DR   EMBL; CP000685; ABQ06186.1; -; Genomic_DNA.
DR   RefSeq; WP_012025155.1; NZ_MUGZ01000015.1.
DR   AlphaFoldDB; A5FF23; -.
DR   SMR; A5FF23; -.
DR   STRING; 376686.Fjoh_3169; -.
DR   EnsemblBacteria; ABQ06186; ABQ06186; Fjoh_3169.
DR   KEGG; fjo:Fjoh_3169; -.
DR   eggNOG; COG2175; Bacteria.
DR   HOGENOM; CLU_722989_0_0_10; -.
DR   OMA; PHTEDAF; -.
DR   OrthoDB; 1742732at2; -.
DR   Proteomes; UP000006694; Chromosome.
DR   GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.130.10; -; 1.
DR   InterPro; IPR042098; TauD-like_sf.
PE   1: Evidence at protein level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..370
FT                   /note="L-lysine 4-hydroxylase"
FT                   /id="PRO_0000435694"
FT   BINDING         176
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z4Z5"
FT   BINDING         178
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z4Z5"
FT   BINDING         310
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z4Z5"
SQ   SEQUENCE   370 AA;  42002 MW;  3CBA6D8DDF599009 CRC64;
     MKSQSLIEDE IPVKENYAYQ IPTSPLIVEV TPQERNILSN VGALLEKAFK SYENPDYIEA
     LHLYSFQLLP ERIARILSRF GTDFSADQYG AIIFRGLLEV DQDHLGPTPA NWQSADYSKL
     NKYGFICSLL HGAVPSKPVQ YYAQRKGGGI LHAVIPDEKM AATQTGSGSK TNLYVHTEDA
     FLLHQADFLS FLYLRNEERV PSTLYSVRSH GKVNKIMEKL FDPIYQCPKD ANYQEEINDG
     PLASVLYGNK KLPFIRFDAA EQIFNENAGQ TPEALYNLTE FWNEAKELIN SDYIPDSGDV
     IFVNNHLCAH GRSAFTAGQK EENGKLVPCE RRQMLRMMSK TSLIHIRSMT HTDDPYFVME
     EHLGKVFDQA