ECTD_HALED
ID ECTD_HALED Reviewed; 332 AA.
AC E1VA04;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 47.
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:20849449};
GN OrderedLocusNames=HELO_4008 {ECO:0000312|EMBL:CBV43892.1};
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS / 1H9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9
RC {ECO:0000312|Proteomes:UP000008707};
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBUNIT.
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
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=4.8 mM for 2-oxoglutarate (at pH 8 and 32 degrees Celsius)
CC {ECO:0000269|PubMed:24714029};
CC KM=5.7 mM for ectoine (at pH 8 and 32 degrees Celsius)
CC {ECO:0000269|PubMed:24714029};
CC Vmax=2.5 umol/min/mg enzyme (at pH 8 and 32 degrees Celsius)
CC {ECO:0000269|PubMed:24714029};
CC Note=kcat is 2.8 sec(-1) for ectoin as substrate (at pH 8 and 32
CC degrees Celsius). {ECO:0000269|PubMed:24714029};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:24714029};
CC Temperature dependence:
CC Optimum temperature is 32 degrees Celsius (PubMed:24714029). Active
CC from 5 to 47 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; FN869568; CBV43892.1; -; Genomic_DNA.
DR RefSeq; WP_013333764.1; NC_014532.2.
DR AlphaFoldDB; E1VA04; -.
DR SMR; E1VA04; -.
DR STRING; 768066.HELO_4008; -.
DR EnsemblBacteria; CBV43892; CBV43892; HELO_4008.
DR KEGG; hel:HELO_4008; -.
DR eggNOG; COG5285; Bacteria.
DR HOGENOM; CLU_048953_5_0_6; -.
DR OMA; MHQFKIN; -.
DR BRENDA; 1.14.11.55; 2569.
DR Proteomes; UP000008707; 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..332
FT /note="Ectoine dioxygenase"
FT /id="PRO_0000445002"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163
FT /ligand="L-ectoine"
FT /ligand_id="ChEBI:CHEBI:58515"
FT /evidence="ECO:0000250|UniProtKB:Q1GNW5"
FT BINDING 169
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q1GNW5"
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT BINDING 182
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT BINDING 281
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q2TDY4"
FT SITE 186
FT /note="Important for ectoine stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q1GNW5"
SQ SEQUENCE 332 AA; 37378 MW; 5C6E8F441BA95356 CRC64;
MSVQTSSNRP LPQANLHIAT ETPEADSRIR SAPRPGQDPY PTRLSEPLDL PWLNRREPVV
KGEEADGPLS AAQLDTFERQ GFIFEPDFLK GEELEALRHE LNALLARDDF RGRDFAITEP
QGNEIRSLFA VHYLSRVFSR LANDERLMGR ARQILGGEPY VHQSRINYKP GFEGKGFNWH
SDFETWHAED GMPAMHAVSA SIVLTDNHTF NGPLMLVPGS HRVFVPCLGE TPEDHHRQSL
KTQEFGVPSR QALRELIDRH GIEAPTGAAG GLLLFDCNTL HGSNANMSPD PRSNAFFVYN
RRDNRCVEPY AASKRRPRFL AHEPDEAWSP DG
