ID   LYS4O_NIAKG             Reviewed;         371 AA.
AC   G8T8D0;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 1.
DT   03-AUG-2022, entry version 42.
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=KDO4 {ECO:0000303|Ref.2};
DE   AltName: Full=L-lysine hydroxylase {ECO:0000303|Ref.2};
GN   OrderedLocusNames=Niako_2766 {ECO:0000312|EMBL:AEV99100.1};
OS   Niastella koreensis (strain DSM 17620 / KACC 11465 / NBRC 106392 /
OS   GR20-10).
OC   Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niastella.
OX   NCBI_TaxID=700598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17620 / KACC 11465 / NBRC 106392 / GR20-10;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Davenport K.,
RA   Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA   Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Niastella koreensis GR20-10.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
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. {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   -!- SIMILARITY: Belongs to the clavaminate synthase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003178; AEV99100.1; -; Genomic_DNA.
DR   RefSeq; WP_014219014.1; NC_016609.1.
DR   AlphaFoldDB; G8T8D0; -.
DR   SMR; G8T8D0; -.
DR   STRING; 700598.Niako_2766; -.
DR   EnsemblBacteria; AEV99100; AEV99100; Niako_2766.
DR   KEGG; nko:Niako_2766; -.
DR   PATRIC; fig|700598.3.peg.2845; -.
DR   eggNOG; COG2175; Bacteria.
DR   HOGENOM; CLU_722989_0_0_10; -.
DR   OMA; PHTEDAF; -.
DR   OrthoDB; 1742732at2; -.
DR   Proteomes; UP000005438; 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; Reference proteome.
FT   CHAIN           1..371
FT                   /note="L-lysine 4-hydroxylase"
FT                   /id="PRO_0000435695"
FT   BINDING         174
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z4Z5"
FT   BINDING         176
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   371 AA;  42080 MW;  82B3AB062262D8FC CRC64;
     METIIESRQR INSPGVLPPP LSPLIVDVTP KERASISNVA NILLKAFGHY EHPDFISALH
     LNAFQLLPER IAGILSRFGT DFSRHQYGAL VFRGLTEVDQ EALGPTPPSW KETDYSKLVK
     YGFICSLLHG AIPSKPVQYY AQRKGGGLLH AVIPDEKMSH TQTGSGSRTD LFVHTEDAFL
     FNQADFLSFL FLRNEEQVPS TLYSIRSHGD TNAIMAELFK PIYKCPKDAN YADDENAGEE
     VTTSILYGNR ERPFIRFDAA EQIYNEKAGQ TPEAMHNLVR FWDEAKQLIY NDFVPDSGDL
     IFVNNHLCAH GRNSFVAGYR NENGQLVKCE RRLMLRMMSK TSLINIQSVT QLNDPYFIME
     EHYGKLFHSQ Q