ECTD_PSEU5
ID ECTD_PSEU5 Reviewed; 302 AA.
AC A4VFY4;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Ectoine dioxygenase {ECO:0000303|PubMed:24714029};
DE EC=1.14.11.55 {ECO:0000269|PubMed:24714029};
DE AltName: Full=Ectoine hydroxylase {ECO:0000303|PubMed:24714029};
GN Name=ectD {ECO:0000303|PubMed:24714029};
GN OrderedLocusNames=PST_0178 {ECO:0000312|EMBL:ABP77885.1};
OS Pseudomonas stutzeri (strain A1501).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=379731;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1501 {ECO:0000312|EMBL:ABP77885.1,
RC ECO:0000312|Proteomes:UP000000233};
RX PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT "Nitrogen fixation island and rhizosphere competence traits in the genome
RT of root-associated Pseudomonas stutzeri A1501.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBUNIT.
RC STRAIN=A1501;
RX PubMed=24714029; DOI=10.1371/journal.pone.0093809;
RA Widderich N., Hoppner A., Pittelkow M., Heider J., Smits S.H., Bremer E.;
RT "Biochemical properties of ectoine hydroxylases from extremophiles and
RT their wider taxonomic distribution among microorganisms.";
RL PLoS ONE 9:e93809-e93809(2014).
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:24714029}.
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:24714029};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:24714029};
CC Note=Binds 1 Fe(2+) ion. {ECO:0000269|PubMed:24714029};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.6 mM for 2-oxoglutarate (at pH 7.5 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:24714029};
CC KM=6.2 mM for ectoine (at pH 7.5 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:24714029};
CC Vmax=6.7 umol/min/mg enzyme (at pH 7.5 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:24714029};
CC Note=kcat is 8.9 sec(-1) for ectoin as substrate (at pH 7.5 and 35
CC degrees Celsius). {ECO:0000269|PubMed:24714029};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:24714029};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius (PubMed:24714029). Active
CC from 10 to 50 degrees Celsius (PubMed:24714029).
CC {ECO:0000269|PubMed:24714029};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24714029}.
CC -!- SIMILARITY: Belongs to the PhyH family. EctD subfamily. {ECO:0000305}.
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DR EMBL; CP000304; ABP77885.1; -; Genomic_DNA.
DR RefSeq; WP_011911424.1; NC_009434.1.
DR AlphaFoldDB; A4VFY4; -.
DR SMR; A4VFY4; -.
DR STRING; 379731.PST_0178; -.
DR EnsemblBacteria; ABP77885; ABP77885; PST_0178.
DR GeneID; 66819451; -.
DR KEGG; psa:PST_0178; -.
DR eggNOG; COG5285; Bacteria.
DR HOGENOM; CLU_048953_5_0_6; -.
DR OMA; FPRSNVF; -.
DR Proteomes; UP000000233; Chromosome.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA: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; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..302
FT /note="Ectoine dioxygenase"
FT /id="PRO_0000445003"
FT BINDING 128
FT /ligand="L-ectoine"
FT /ligand_id="ChEBI:CHEBI:58515"
FT /evidence="ECO:0000250|UniProtKB:Q1GNW5"
FT BINDING 134
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q1GNW5"
FT BINDING 145
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT BINDING 246
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT SITE 151
FT /note="Important for ectoine stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q1GNW5"
SQ SEQUENCE 302 AA; 34184 MW; 4B1A891EA1D37851 CRC64;
MQADLYPSRQ EDQPSWQERL DPVVYRSDLE NAPIAAELVE RFERDGYLVI PNLFSADEVA
LFRAELERMR QDPAVAGSGK TIKEPDSGAI RSVFAIHKDN ELFARVAADE RTAGIARFIL
GGDLYVHQSR MNFKPGFTGK EFYWHSDFET WHIEDGMPRM RCLSCSILLT DNEPHNGPLM
LMPGSHKHYV RCVGATPENH YEKSLRKQEI GIPDQNSLSE LASRFGIDCA TGPAGSVVFF
DCNTMHGSNG NITPSARSNL FYVYNHVDNA VQAPFCEQKP RPAFVAEREN FKPLDIRPQQ
YL
