ID   ECTD_STRAW              Reviewed;         295 AA.
AC   Q829L6;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Ectoine dioxygenase {ECO:0000250|UniProtKB:Q93RV9};
DE            EC=1.14.11.55 {ECO:0000250|UniProtKB:Q93RV9};
DE   AltName: Full=Ectoine hydroxylase {ECO:0000250|UniProtKB:Q93RV9};
GN   Name=ectD {ECO:0000250|UniProtKB:Q93RV9}; OrderedLocusNames=SAV_6395;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS   14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA   Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT   deducing the ability of producing secondary metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(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:Q93RV9}.
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:Q93RV9};
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:Q93RV9}.
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DR   EMBL; BA000030; BAC74106.2; -; Genomic_DNA.
DR   RefSeq; WP_037646868.1; NZ_JZJK01000089.1.
DR   AlphaFoldDB; Q829L6; -.
DR   SMR; Q829L6; -.
DR   STRING; 227882.SAV_6395; -.
DR   EnsemblBacteria; BAC74106; BAC74106; SAVERM_6395.
DR   KEGG; sma:SAVERM_6395; -.
DR   eggNOG; COG5285; Bacteria.
DR   HOGENOM; CLU_048953_5_0_11; -.
DR   OMA; FPRSNVF; -.
DR   OrthoDB; 1070946at2; -.
DR   Proteomes; UP000000428; 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; Reference proteome.
FT   CHAIN           1..295
FT                   /note="Ectoine dioxygenase"
FT                   /id="PRO_0000215241"
FT   BINDING         129
FT                   /ligand="L-ectoine"
FT                   /ligand_id="ChEBI:CHEBI:58515"
FT                   /evidence="ECO:0000250|UniProtKB:Q1GNW5"
FT   BINDING         135
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:Q1GNW5"
FT   BINDING         146
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT   BINDING         148
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT   BINDING         247
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT   SITE            152
FT                   /note="Important for ectoine stabilization"
FT                   /evidence="ECO:0000250|UniProtKB:Q1GNW5"
SQ   SEQUENCE   295 AA;  32618 MW;  7788167998D2F407 CRC64;
     MTTITDLYPS RGAAEVSVPR QDPVLWGTPD TPGPITAADL QSYEHDGFLA VPQLIGDDEV
     ALYHAELERL IHDPAVRADE RSIVEPQSQE IRSVFEVHKI SEIFAQLVRD ERVVGRARQI
     LGSDVYVHQS RINVKPGFGA SGFYWHSDFE TWHAEDGLPN MRTVSVSIAL TENYDTNGGL
     MIMPGSHKTF LGCAGATPKD NYKKSLQMQD AGTPSDEALT KFADRHGIRL FTGRAGSATW
     FDCNCLHGSG DNITPFPRSN VFIVFNSVEN TAVEPFSAPV RRPEFIGARD FTPVR