ECTC_HALED
ID ECTC_HALED Reviewed; 137 AA.
AC O52251; E1VCW9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=L-ectoine synthase;
DE EC=4.2.1.108 {ECO:0000269|PubMed:9864317};
DE AltName: Full=N-acetyldiaminobutyrate dehydratase;
GN Name=ectC; OrderedLocusNames=HELO_2590;
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;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9;
RX PubMed=9570121; DOI=10.1111/j.1574-6968.1998.tb12960.x;
RA Goeller K., Ofer A., Galinski E.A.;
RT "Construction and characterization of an NaCl-sensitive mutant of Halomonas
RT elongata impaired in ectoine biosynthesis.";
RL FEMS Microbiol. Lett. 161:293-300(1998).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP CHARACTERIZATION.
RC STRAIN=OUT30018;
RX PubMed=9864317; DOI=10.1128/jb.181.1.91-99.1999;
RA Ono H., Sawada K., Khunajakr N., Tao T., Yamamoto M., Hiramoto M.,
RA Shinmyo A., Takano M., Murooka Y.;
RT "Characterization of biosynthetic enzymes for ectoine as a compatible
RT solute in a moderately halophilic eubacterium, Halomonas elongata.";
RL J. Bacteriol. 181:91-99(1999).
CC -!- FUNCTION: Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-
CC diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-
CC pyrimidine carboxylic acid), which is an excellent osmoprotectant. Does
CC not act on N-acetylated amino acids like N-alpha-acetyl-L-asparagine,N-
CC alpha-acetyl-L-ornithine, N-alpha-acetyl-L-lysine and N-epsilon-acetyl-
CC L-lysine. {ECO:0000269|PubMed:9864317}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-4-acetamido-2-aminobutanoate = H2O + L-ectoine;
CC Xref=Rhea:RHEA:17281, ChEBI:CHEBI:15377, ChEBI:CHEBI:58515,
CC ChEBI:CHEBI:58929; EC=4.2.1.108;
CC Evidence={ECO:0000269|PubMed:9864317};
CC -!- ACTIVITY REGULATION: Seems to require potassium ions for its activity
CC and stability. Slightly inhibited by N-ethylmaleimide.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 mM for ADABA (in the presence of 0.05 M NaCl)
CC {ECO:0000269|PubMed:9864317};
CC KM=8.4 mM for ADABA (in the presence of 0.77 M NaCl)
CC {ECO:0000269|PubMed:9864317};
CC Vmax=85 umol/min/mg enzyme (in the presence of 0.05 M NaCl)
CC {ECO:0000269|PubMed:9864317};
CC Vmax=56 umol/min/mg enzyme (in the presence of 0.77 M NaCl)
CC {ECO:0000269|PubMed:9864317};
CC pH dependence:
CC Optimum pH is 8.5-9.0. {ECO:0000269|PubMed:9864317};
CC Temperature dependence:
CC Optimum temperature is 0-10 degrees Celsius in the presence of 0.05 M
CC NaCl, 15 degrees Celsius in the presence of 0.77 M NaCl, and 30
CC degrees Celsius in the presence of 3.0 M NaCl.
CC {ECO:0000269|PubMed:9864317};
CC -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC ectoine from L-aspartate 4-semialdehyde: step 3/3.
CC -!- SIMILARITY: Belongs to the ectoine synthase family. {ECO:0000305}.
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DR EMBL; FN869568; CBV42474.1; -; Genomic_DNA.
DR EMBL; AF031489; AAC15883.1; -; Genomic_DNA.
DR RefSeq; WP_013332346.1; NC_014532.2.
DR AlphaFoldDB; O52251; -.
DR SMR; O52251; -.
DR STRING; 768066.HELO_2590; -.
DR EnsemblBacteria; CBV42474; CBV42474; HELO_2590.
DR KEGG; hel:HELO_2590; -.
DR eggNOG; COG1917; Bacteria.
DR HOGENOM; CLU_154525_0_0_6; -.
DR OMA; CVFNPPI; -.
DR BioCyc; MetaCyc:MON-803; -.
DR UniPathway; UPA00067; UER00123.
DR Proteomes; UP000008707; Chromosome.
DR GO; GO:0033990; F:ectoine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019491; P:ectoine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06978; cupin_EctC; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR HAMAP; MF_01255; Ectoine_synth; 1.
DR InterPro; IPR010462; Ectoine_synth.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR39289; PTHR39289; 1.
DR Pfam; PF06339; Ectoine_synth; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW Lyase; Reference proteome.
FT CHAIN 1..137
FT /note="L-ectoine synthase"
FT /id="PRO_0000220152"
FT REGION 118..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 137 AA; 15458 MW; B13EA0FA6F2F3F27 CRC64;
MIVRNLEEAR QTDRLVTAEN GNWDSTRLSL AEDGGNCSFH ITRIFEGTET HIHYKHHFEA
VYCIEGEGEV ETLADGKIWP IKPGDIYILD QHDEHLLRAS KTMHLACVFT PGLTGNEVHR
EDGSYAPADE ADDQKPL
