ORR3O_CATAD
ID ORR3O_CATAD Reviewed; 343 AA.
AC C7Q942;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=L-ornithine/L-arginine 3-hydroxylase {ECO:0000305|Ref.2};
DE EC=1.14.11.- {ECO:0000269|Ref.2};
DE EC=1.14.11.41 {ECO:0000269|Ref.2};
DE AltName: Full=Alpha-ketoglutarate-dependent dioxygenase {ECO:0000303|Ref.2};
DE AltName: Full=L-ornithine/L-arginine hydroxylase {ECO:0000303|Ref.2};
DE AltName: Full=ODO {ECO:0000303|Ref.2};
GN OrderedLocusNames=Caci_3456 {ECO:0000312|EMBL:ACU72362.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC Catenulispora.
OX NCBI_TaxID=479433;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908;
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., 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 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-ornithine
CC and L-arginine, leading to (3S)-3-hydroxy-L-ornithine and (3S)-3-
CC hydroxy-L-arginine, respectively. Cannot use L-lysine, D-ornithine, or
CC D-arginine as substrate. {ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-ornithine + O2 = (3S)-3-hydroxy-L-ornithine
CC + CO2 + succinate; Xref=Rhea:RHEA:40931, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:77411; Evidence={ECO:0000269|Ref.2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-arginine + O2 = (2S,3S)-hydroxyarginine +
CC CO2 + succinate; Xref=Rhea:RHEA:36607, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:32682, ChEBI:CHEBI:73938; EC=1.14.11.41;
CC 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; CP001700; ACU72362.1; -; Genomic_DNA.
DR RefSeq; WP_012787655.1; NC_013131.1.
DR AlphaFoldDB; C7Q942; -.
DR SMR; C7Q942; -.
DR STRING; 479433.Caci_3456; -.
DR EnsemblBacteria; ACU72362; ACU72362; Caci_3456.
DR KEGG; cai:Caci_3456; -.
DR eggNOG; COG2175; Bacteria.
DR HOGENOM; CLU_044078_0_0_11; -.
DR OMA; FIDNFRA; -.
DR OrthoDB; 1742732at2; -.
DR Proteomes; UP000000851; Chromosome.
DR GO; GO:0102525; F:2-oxoglutarate, L-arginine oxygenase (succinate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR023966; Arginine_beta-hydroxylase.
DR InterPro; IPR014503; Clavaminate_syn-like.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF02668; TauD; 1.
DR PIRSF; PIRSF019543; Clavaminate_syn; 1.
DR TIGRFAMs; TIGR03946; viomycin_VioC; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..343
FT /note="L-ornithine/L-arginine 3-hydroxylase"
FT /id="PRO_0000435697"
FT REGION 199..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4Z5"
FT BINDING 149
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4Z5"
FT BINDING 302
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4Z5"
FT BINDING 316
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4Z5"
SQ SEQUENCE 343 AA; 39116 MW; A8CBD5ED9EEE22AF CRC64;
MHRLALTAQD NLAVAPMLAD LAGRYPDIED PELIRSAPVL AAKGLPPHLL AFLDDFRLRE
PSALCVISGL DVDQDRLGPT PEHWRDSQIG SRSLNLEIFF LLCGAALGDV FGWATQQDGR
IMHDVLPIKG HEHYELGSNS LQHLSWHTED SFHPCRGDYV ALMCLKNPYE AETMVCDAGD
LDWPNLDVDA LFEPVFTQMP DNSHLPQNTA ESTGDPTKDR LRARSFELIK SWNENPVRRA
VLYGDRQNPY MALDPYHMKM DDWSERSLEA FQALCEEIEA KMQDVVLHPG DIAFIDNFRA
VHGRRSFRAR YDGSDRWLKR LNITRNLRGS RAWRPAPDDR VIY
