ID   ECTC_CHRSD              Reviewed;         130 AA.
AC   Q9ZEU6; Q1QWC8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=L-ectoine synthase;
DE            EC=4.2.1.108;
DE   AltName: Full=N-acetyldiaminobutyrate dehydratase;
GN   Name=ectC; OrderedLocusNames=Csal_1878;
OS   Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS   NCIMB 13768 / 1H11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9924816; DOI=10.1016/s0723-2020(98)80060-x;
RA   Canovas D., Vargas C., Calderon M.I., Ventosa A., Nieto J.J.;
RT   "Characterization of the genes for the biosynthesis of the compatible
RT   solute ectoine in the moderately halophilic bacterium Halomonas elongata
RT   DSM 3043.";
RL   Syst. Appl. Microbiol. 21:487-497(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX   PubMed=22675587; DOI=10.4056/sigs.2285059;
RA   Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA   Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT   "Complete genome sequence of the halophilic and highly halotolerant
RT   Chromohalobacter salexigens type strain (1H11(T)).";
RL   Stand. Genomic Sci. 5:379-388(2011).
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.
CC       {ECO:0000250}.
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   -!- 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; AJ011103; CAA09485.1; -; Genomic_DNA.
DR   EMBL; CP000285; ABE59230.1; -; Genomic_DNA.
DR   RefSeq; WP_011507176.1; NC_007963.1.
DR   AlphaFoldDB; Q9ZEU6; -.
DR   SMR; Q9ZEU6; -.
DR   STRING; 290398.Csal_1878; -.
DR   DNASU; 4028241; -.
DR   EnsemblBacteria; ABE59230; ABE59230; Csal_1878.
DR   KEGG; csa:Csal_1878; -.
DR   eggNOG; COG1917; Bacteria.
DR   HOGENOM; CLU_154525_0_0_6; -.
DR   OMA; CVFNPPI; -.
DR   OrthoDB; 1928636at2; -.
DR   BRENDA; 4.2.1.108; 8057.
DR   UniPathway; UPA00067; UER00123.
DR   Proteomes; UP000000239; 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   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..130
FT                   /note="L-ectoine synthase"
FT                   /id="PRO_0000220151"
SQ   SEQUENCE   130 AA;  14825 MW;  EE0E0B30B1E761BE CRC64;
     MIVRNLEECR KTERFVEAEN GNWDSTRLVL ADDNVGFSFN ITRIHPGTET HIHYKHHFEA
     VFCYEGEGEV ETLADGKIHP IKAGDMYLLD QHDEHLLRGK EKGMTVACVF NPALTGREVH
     REDGSYAPVD