ID   ECTD_BORBR              Reviewed;         308 AA.
AC   Q7WHJ0;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Ectoine dioxygenase {ECO:0000250|UniProtKB:Q2TDY4};
DE            EC=1.14.11.55 {ECO:0000250|UniProtKB:Q2TDY4};
DE   AltName: Full=Ectoine hydroxylase {ECO:0000250|UniProtKB:Q2TDY4};
GN   Name=ectD {ECO:0000250|UniProtKB:Q2TDY4}; OrderedLocusNames=BB3217;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Involved in the biosynthesis of 5-hydroxyectoine, called
CC       compatible solute, which helps organisms to survive extreme osmotic
CC       stress by acting as a highly soluble organic osmolyte. Catalyzes the 2-
CC       oxoglutarate-dependent selective hydroxylation of L-ectoine to yield
CC       (4S,5S)-5-hydroxyectoine. {ECO:0000250|UniProtKB:Q2TDY4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-ectoine + O2 = 5-hydroxyectoine + CO2 +
CC         succinate; Xref=Rhea:RHEA:45740, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:58515, ChEBI:CHEBI:85413; EC=1.14.11.55;
CC         Evidence={ECO:0000250|UniProtKB:Q2TDY4};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q2TDY4};
CC       Note=Binds 1 Fe(2+) ion. {ECO:0000250|UniProtKB:Q2TDY4};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q2TDY4}.
CC   -!- SIMILARITY: Belongs to the PhyH family. EctD subfamily.
CC       {ECO:0000250|UniProtKB:Q2TDY4}.
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DR   EMBL; BX640446; CAE33709.1; -; Genomic_DNA.
DR   RefSeq; WP_003818667.1; NC_002927.3.
DR   AlphaFoldDB; Q7WHJ0; -.
DR   SMR; Q7WHJ0; -.
DR   STRING; 257310.BB3217; -.
DR   EnsemblBacteria; CAE33709; CAE33709; BB3217.
DR   KEGG; bbr:BB3217; -.
DR   eggNOG; COG5285; Bacteria.
DR   HOGENOM; CLU_048953_5_0_4; -.
DR   OMA; FPRSNVF; -.
DR   OrthoDB; 1070946at2; -.
DR   Proteomes; UP000001027; Chromosome.
DR   GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR   GO; GO:0042400; P:ectoine catabolic process; ISS:UniProtKB.
DR   InterPro; IPR012774; EctD.
DR   InterPro; IPR008775; Phytyl_CoA_dOase.
DR   Pfam; PF05721; PhyH; 1.
DR   TIGRFAMs; TIGR02408; ectoine_ThpD; 1.
PE   3: Inferred from homology;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..308
FT                   /note="Ectoine dioxygenase"
FT                   /id="PRO_0000215238"
FT   BINDING         131
FT                   /ligand="L-ectoine"
FT                   /ligand_id="ChEBI:CHEBI:58515"
FT                   /evidence="ECO:0000250|UniProtKB:Q1GNW5"
FT   BINDING         137
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q1GNW5"
FT   BINDING         148
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT   BINDING         150
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT   BINDING         249
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT   SITE            154
FT                   /note="Important for ectoine stabilization"
FT                   /evidence="ECO:0000250|UniProtKB:Q1GNW5"
SQ   SEQUENCE   308 AA;  34382 MW;  B9A105865BDF354D CRC64;
     MISPAQDPYA SRTDRSSAII ARQDPVVYGE GKFADALSAD QVQSYERDGF LLLENLFSDE
     EVAALLAEVE RMTRDPAIVR REEAITEPGS NAVRSIFMVH VLSPILGRLV RDPRLANAAR
     QILGSEVYVH QSRANMKPGF KGKEFYWHSD FETWHVEDGM PSMRALSCSV LLTDNNETNG
     PLMLVPGSHR QFISCVGETP RDHYKQSLKK QEYGVPDPVS LQLLAEQGGI STMTGKAGSV
     VFFDCNTMHG SNSNISPWPR ANVFMVYNSM ENTLNPPKYG LNPRPEHIAT RQAFKAVRPL
     DSLKLVER