(data stored in ACNUC7421 zone)

SWISSPROT: LYS3O_CATAD

ID   LYS3O_CATAD             Reviewed;         358 AA.
AC   C7QJ42;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   05-JUL-2017, entry version 42.
DE   RecName: Full=L-lysine 3-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=KDO1 {ECO:0000303|Ref.2};
DE   AltName: Full=L-lysine hydroxylase {ECO:0000303|Ref.2};
GN   OrderedLocusNames=Caci_0231 {ECO:0000312|EMBL:ACU69184.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897;
RX   PubMed=21304647; DOI=10.4056/sigs.17259;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND
RP   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.,
RA   Salanoubat M., 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-
CC       lysine, leading to (3S)-3-hydroxy-L-lysine. Can also use (5R)-5-
CC       hydroxy-L-lysine as substrate, but neither D-lysine nor L-
CC       ornithine. {ECO:0000269|Ref.2}.
CC   -!- CATALYTIC ACTIVITY: L-lysine + 2-oxoglutarate + O(2) = (3S)-3-
CC       hydroxy-L-lysine + succinate + CO(2). {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.
CC       {ECO:0000250|UniProtKB:Q9Z4Z5};
CC   -!- BIOTECHNOLOGY: Being totally regio- and stereoselective, this
CC       enzyme is of interest for biocatalytic purposes to produce chiral
CC       scaffolds that are of synthetic value in the preparation of more
CC       complex functionalized chiral molecules such as natural products
CC       and analogs. {ECO:0000305|Ref.2}.
CC   -!- SIMILARITY: Belongs to the clavaminate synthase family.
CC       {ECO:0000305}.
DR   EMBL; CP001700; ACU69184.1; -; Genomic_DNA.
DR   RefSeq; WP_012784479.1; NC_013131.1.
DR   SMR; C7QJ42; -.
DR   STRING; 479433.Caci_0231; -.
DR   EnsemblBacteria; ACU69184; ACU69184; Caci_0231.
DR   KEGG; cai:Caci_0231; -.
DR   eggNOG; ENOG4105MVH; Bacteria.
DR   eggNOG; ENOG4111VTW; LUCA.
DR   HOGENOM; HOG000000273; -.
DR   OMA; VHTEDAF; -.
DR   OrthoDB; POG091H0FFQ; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IDA:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
DR   InterPro; IPR014503; Clavaminate_syn-like.
DR   InterPro; IPR003819; TauD/TfdA-like.
DR   Pfam; PF02668; TauD; 1.
DR   PIRSF; PIRSF019543; Clavaminate_syn; 1.
PE   1: Evidence at protein level;
DR   PRODOM; C7QJ42.
DR   SWISS-2DPAGE; C7QJ42.
KW   Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    358       L-lysine 3-hydroxylase.
FT                                /FTId=PRO_0000435692.
FT   METAL       178    178       Iron. {ECO:0000250|UniProtKB:Q9Z4Z5}.
FT   METAL       180    180       Iron. {ECO:0000250|UniProtKB:Q9Z4Z5}.
FT   METAL       314    314       Iron. {ECO:0000250|UniProtKB:Q9Z4Z5}.
FT   BINDING     328    328       2-oxoglutarate.
FT                                {ECO:0000250|UniProtKB:Q9Z4Z5}.
SQ   SEQUENCE   358 AA;  39194 MW;  1687DA44FCD2B917 CRC64;
     MKNLSAYEVY ESPKTSGESR TEAVSEAAFE SDPEVSAILV LTSSEASTLE RVADLVTAHA
     LYAAHDFCAQ AQLAAAELPS RVVARLQEFA WGDMNEGHLL IKGLPQVRSL PPTPTSNVHA
     VAATTPMSRY QALINECVGR MIAYEAEGHG HTFQDMVPSA MSAHSQTSLG SAVELELHTE
     QAFSPLRPDF VSLACLRGDP RALTYLFSAR QLVATLTTQE IAMLREPMWT TTVDESFLAE
     GRTFLLGFER GPIPILSGAD DDPFIVFDQD LMRGISAPAQ ELQQTVIRAY YAERVSHCLA
     PGEMLLIDNR RAVHGRSIFA PRFDGADRFL SRSFIVADGS RSRHARSSFG RVVSARFS
//

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