ID   ECTD_STRAQ              Reviewed;         297 AA.
AC   Q6QUY7;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 51.
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}; Synonyms=thpD;
OS   Streptomyces anulatus (Streptomyces chrysomallus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1892;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 11523 / DSM 40128 / JCM 4296 / LMG 20459 / NBRC 15393;
RX   PubMed=15128576; DOI=10.1128/aem.70.5.3130-3132.2004;
RA   Prabhu J., Schauwecker F., Grammel N., Keller U., Bernhard M.;
RT   "Functional expression of the ectoine hydroxylase gene (thpD) from
RT   Streptomyces chrysomallus in Halomonas elongata.";
RL   Appl. Environ. Microbiol. 70:3130-3132(2004).
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:0000269|PubMed:15128576}.
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. {ECO:0000305}.
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DR   EMBL; AY524544; AAS02097.1; -; Genomic_DNA.
DR   RefSeq; WP_056706218.1; NZ_CM003601.1.
DR   AlphaFoldDB; Q6QUY7; -.
DR   SMR; Q6QUY7; -.
DR   PRIDE; Q6QUY7; -.
DR   BRENDA; 1.14.11.55; 5994.
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..297
FT                   /note="Ectoine dioxygenase"
FT                   /id="PRO_0000215242"
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   297 AA;  32689 MW;  FC2FBBC1C49A8EBA CRC64;
     MTTEVRADLY PSRGAAEMTT PRQDPVIWSA PGAPGPVAAK DLQGYEHDGF LTVDQLIAPD
     EVAVYQAELN RLISDPAVRA DERSIVEKQS QNVRSVFEVH RISEVFAGLV RDERVVGRAR
     QILGSDVYVH QSRINVKPGF GATGFYWHSD FETWHAEDGL PNMRTVSVSI ALTENFDTNG
     GLMIMPGSHK TFLGCAGETP KDNYKKSLQM QDAGTPSDEA LTKMADRHGI RLFTGRAGSA
     TWFDCNAMHG SGDNITPYAR SNVFIVFNSV ENAAQEPFAA PIRRPEFIGA RDFTPVK