LYS4O_FLASC
ID LYS4O_FLASC Reviewed; 372 AA.
AC J3BZS6;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 40.
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=KDO5 {ECO:0000303|Ref.2};
DE AltName: Full=L-lysine hydroxylase {ECO:0000303|Ref.2};
GN ORFNames=PMI10_03368 {ECO:0000312|EMBL:EJL61441.1};
OS Flavobacterium sp. (strain CF136).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium; unclassified Flavobacterium.
OX NCBI_TaxID=1144313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF136;
RX PubMed=23045501; DOI=10.1128/jb.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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}.
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DR EMBL; AKJZ01000057; EJL61441.1; -; Genomic_DNA.
DR RefSeq; WP_007810048.1; NZ_AKJZ01000057.1.
DR PDB; 6EUO; X-ray; 2.30 A; A/B/C/D=1-372.
DR PDB; 6EUR; X-ray; 2.30 A; A/B/C/D=1-372.
DR PDB; 6EXF; X-ray; 1.95 A; A/B/C/D=1-372.
DR PDB; 6EXH; X-ray; 2.60 A; A/B/C/D=1-372.
DR PDB; 6F9P; X-ray; 2.40 A; A/B/C/D=1-372.
DR PDBsum; 6EUO; -.
DR PDBsum; 6EUR; -.
DR PDBsum; 6EXF; -.
DR PDBsum; 6EXH; -.
DR PDBsum; 6F9P; -.
DR AlphaFoldDB; J3BZS6; -.
DR SMR; J3BZS6; -.
DR STRING; 1144313.PMI10_03368; -.
DR EnsemblBacteria; EJL61441; EJL61441; PMI10_03368.
DR PATRIC; fig|1144313.4.peg.3352; -.
DR eggNOG; COG2175; Bacteria.
DR OMA; PHTEDAF; -.
DR Proteomes; UP000007287; Unassembled WGS sequence.
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 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..372
FT /note="L-lysine 4-hydroxylase"
FT /id="PRO_0000435696"
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 312
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4Z5"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:6EXF"
FT HELIX 32..49
FT /evidence="ECO:0007829|PDB:6EXF"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:6EXF"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:6EXF"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:6EXF"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:6EXF"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:6EXF"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:6EXF"
FT HELIX 117..132
FT /evidence="ECO:0007829|PDB:6EXF"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6EXF"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:6EXF"
FT TURN 142..146
FT /evidence="ECO:0007829|PDB:6EXF"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6EXF"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6EXF"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:6EXF"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:6EUO"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:6EXF"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:6EXF"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:6EXF"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:6EXF"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:6EXF"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:6EXF"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:6EXF"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:6EXF"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:6EXF"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:6EUO"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:6EXF"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:6EXF"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:6EXF"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:6EXF"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:6EXF"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:6EXF"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:6EXF"
FT STRAND 335..343
FT /evidence="ECO:0007829|PDB:6EXF"
FT TURN 345..348
FT /evidence="ECO:0007829|PDB:6EXF"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:6EXF"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:6EXF"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:6EXF"
SQ SEQUENCE 372 AA; 41773 MW; 61447DA3823A54D2 CRC64;
MKSQSIMSVE RSAETSLTLE IPTSPLIIKI TQQERNILSN VGNLLVKAFG NYENPDYIAS
LHLHAFQLLP ERITRILSQF GSDFSAEQYG AIVFQGLIEV DQDDLGPTPP NWQGADYGKL
NKYGFICSLL HGAVPSKPVQ YYAQRKGGGL LHAVIPDEKM AATQTGSGSK TDLFVHTEDA
FLSNQADFLS FLYLRNEERV PSTLYSIRSH GKMNPVMKKL FEPIYQCPKD ANYNDEDVAN
SGPTASVLYG NRELPFIRFD AAEQIFNENA GQTSEALGNL MDFWDEAKTL INSDYIPNSG
DLIFVNNHLC AHGRSAFIAG QRIENGEIIK CERRQMLRMM SKTSLIHIRS VTRTDDPYFI
MEEHLGKIFD LD
