ID   LYS4O_CHIPD             Reviewed;         382 AA.
AC   C7PLM6;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
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=KDO2 {ECO:0000303|Ref.2};
DE   AltName: Full=L-lysine hydroxylase {ECO:0000303|Ref.2};
GN   OrderedLocusNames=Cpin_2834 {ECO:0000312|EMBL:ACU60313.1};
OS   Chitinophaga pinensis (strain ATCC 43595 / DSM 2588 / LMG 13176 / NBRC
OS   15968 / NCIMB 11800 / UQM 2034).
OC   Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=485918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43595 / DSM 2588 / LMG 13176 / NBRC 15968 / NCIMB 11800 / UQM
RC   2034;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Sims D., Meinche L., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Spring S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Chitinophaga pinensis DSM 2588.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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. Cannot use D-lysine or L-ornithine
CC       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; CP001699; ACU60313.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7PLM6; -.
DR   SMR; C7PLM6; -.
DR   STRING; 485918.Cpin_2834; -.
DR   EnsemblBacteria; ACU60313; ACU60313; Cpin_2834.
DR   KEGG; cpi:Cpin_2834; -.
DR   eggNOG; COG2175; Bacteria.
DR   HOGENOM; CLU_722989_0_0_10; -.
DR   OMA; PHTEDAF; -.
DR   Proteomes; UP000002215; 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..382
FT                   /note="L-lysine 4-hydroxylase"
FT                   /id="PRO_0000435693"
FT   BINDING         182
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z4Z5"
FT   BINDING         184
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z4Z5"
FT   BINDING         318
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z4Z5"
SQ   SEQUENCE   382 AA;  43561 MW;  88D3F08C74C39B68 CRC64;
     MRPLDVTPTI SPGAQDLPRT MHFAAEPPLQ PLIIDITEEE KLEITYIGKK LKRKYKSYDD
     PGFISMLHLN AYTLLPERIA KVLSNFGTDF SDQQYGAVVL RGLIEIGQDE LGPTPRSWQE
     TDHEKIMEYG FISSLLHGAV PSKPVEYFAQ RKGGGLMHAI IPDENMSFTQ TGSGSRTDLF
     VHTEDAFLHN AADFLSFLFL RNEERVPSTL YSIRSHGRPD AILQELFKPI YKCPKDANYA
     SEEALGDDIR TSVLYGSRSA PFMRFDAAEQ IYNEDANQDP EALHNLKRFW EEARKLIYND
     FVPESGDLIF VNNHLCAHGR NAFLAGFREE NGQLVKCERR LMLRMMSKTS LINIREVTHP
     ENPYLIMEEH YGKVYSAHLA NL