ECTD_STRCO
ID ECTD_STRCO Reviewed; 299 AA.
AC Q93RV9;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Ectoine dioxygenase {ECO:0000303|PubMed:18849444};
DE EC=1.14.11.55 {ECO:0000269|PubMed:18849444};
DE AltName: Full=Ectoine hydroxylase {ECO:0000303|PubMed:18849444};
GN Name=ectD {ECO:0000303|PubMed:18849444}; OrderedLocusNames=SCO1867;
GN ORFNames=SCI39.14;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP PROTEIN SEQUENCE OF 1-11, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=18849444; DOI=10.1128/aem.00768-08;
RA Bursy J., Kuhlmann A.U., Pittelkow M., Hartmann H., Jebbar M., Pierik A.J.,
RA Bremer E.;
RT "Synthesis and uptake of the compatible solutes ectoine and 5-
RT hydroxyectoine by Streptomyces coelicolor A3(2) in response to salt and
RT heat stresses.";
RL Appl. Environ. Microbiol. 74:7286-7296(2008).
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:18849444}.
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:0000269|PubMed:18849444};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 mM for ectoine {ECO:0000269|PubMed:18849444};
CC KM=6.2 mM for 2-oxoglutarate {ECO:0000269|PubMed:18849444};
CC Vmax=20 umol/min/mg enzyme {ECO:0000269|PubMed:18849444};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:18849444};
CC Temperature dependence:
CC Optimum temperature is 32 degrees Celsius.
CC {ECO:0000269|PubMed:18849444};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q2TDY4}.
CC -!- SIMILARITY: Belongs to the PhyH family. EctD subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC38802.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL939110; CAC38802.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_626134.1; NC_003888.3.
DR RefSeq; WP_003976953.1; NZ_CP042324.1.
DR AlphaFoldDB; Q93RV9; -.
DR SMR; Q93RV9; -.
DR STRING; 100226.SCO1867; -.
DR GeneID; 1097301; -.
DR KEGG; sco:SCO1867; -.
DR PATRIC; fig|100226.15.peg.1892; -.
DR eggNOG; COG5285; Bacteria.
DR HOGENOM; CLU_048953_5_0_11; -.
DR InParanoid; Q93RV9; -.
DR PhylomeDB; Q93RV9; -.
DR Proteomes; UP000001973; 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 1: Evidence at protein level;
KW Dioxygenase; Direct protein sequencing; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..299
FT /note="Ectoine dioxygenase"
FT /id="PRO_0000215243"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133
FT /ligand="L-ectoine"
FT /ligand_id="ChEBI:CHEBI:58515"
FT /evidence="ECO:0000250|UniProtKB:Q1GNW5"
FT BINDING 139
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q1GNW5"
FT BINDING 150
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT BINDING 152
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT BINDING 251
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT SITE 156
FT /note="Important for ectoine stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q1GNW5"
SQ SEQUENCE 299 AA; 32866 MW; D45368191DAE307E CRC64;
MTTTTTNVTD LYPTRGATEV ATPRQDPVVW GSPDAPGPVS AGDLQALDRD GFLAIDQLIT
PDEVGEYQRE LERLTTDPAI RADERSIVEP QSKEIRSVFE VHKISEVFAK LVRDERVVGR
ARQILGSDVY VHQSRINVKP GFGASGFYWH SDFETWHAED GLPNMRTISV SIALTENYDT
NGGLMIMPGS HKTFLGCAGA TPKDNYKKSL QMQDAGTPSD EGLTKMASEY GIKLFTGKAG
SATWFDCNCM HGSGDNITPF PRSNVFIVFN SVENTAVEPF AAPIRRPEFI GARDFTPVK
