ECTD_BORPA
ID ECTD_BORPA Reviewed; 308 AA.
AC Q7W977;
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=BPP1891;
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX640428; CAE37192.1; -; Genomic_DNA.
DR RefSeq; WP_010928264.1; NC_002928.3.
DR AlphaFoldDB; Q7W977; -.
DR SMR; Q7W977; -.
DR EnsemblBacteria; CAE37192; CAE37192; BPP1891.
DR KEGG; bpa:BPP1891; -.
DR HOGENOM; CLU_048953_5_0_4; -.
DR OMA; FPRSNVF; -.
DR Proteomes; UP000001421; 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_0000215239"
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; 34336 MW; 2BAA719D35AF2740 CRC64;
MISPAQDPYA SRTDRSSAII ARQDPVVYGE GKFADALSAD QVQSYERDGF LLLENLFSDE
EVAALLAEVE RMTRDPAIVR REEAITEPGS NAVRSIFMVH VLSPILGRLV RDPRLANAAR
QILGAEVYVH QSRANMKPGF KGKEFYWHSD FETWHVEDGM PSMRALSCSV LLTDNNEANG
PLMLVPGSHR QFISCVGETP RDHYKQSLKK QEYGVPDPVS LQLLAEQGGI STMTGKAGSV
VFFDCNTMHG SNSNISPWPR ANVFMVYNSM ENTLNPPKYG LNPRPEHIAT RQAFKAVRPL
DSLKLVER