ID   ECTC_ALKCK              Reviewed;         134 AA.
AC   Q5WL77;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=L-ectoine synthase {ECO:0000255|HAMAP-Rule:MF_01255};
DE            EC=4.2.1.108 {ECO:0000255|HAMAP-Rule:MF_01255};
DE   AltName: Full=N-acetyldiaminobutyrate dehydratase {ECO:0000255|HAMAP-Rule:MF_01255};
GN   Name=ectC {ECO:0000255|HAMAP-Rule:MF_01255}; OrderedLocusNames=ABC0336;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_01255}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01255};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC       ectoine from L-aspartate 4-semialdehyde: step 3/3. {ECO:0000255|HAMAP-
CC       Rule:MF_01255}.
CC   -!- SIMILARITY: Belongs to the ectoine synthase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01255}.
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DR   EMBL; AP006627; BAD62878.1; -; Genomic_DNA.
DR   RefSeq; WP_011245197.1; NC_006582.1.
DR   AlphaFoldDB; Q5WL77; -.
DR   SMR; Q5WL77; -.
DR   STRING; 66692.ABC0336; -.
DR   EnsemblBacteria; BAD62878; BAD62878; ABC0336.
DR   GeneID; 61572786; -.
DR   KEGG; bcl:ABC0336; -.
DR   eggNOG; COG1917; Bacteria.
DR   HOGENOM; CLU_154525_0_0_9; -.
DR   OMA; CVFNPPI; -.
DR   OrthoDB; 1928636at2; -.
DR   UniPathway; UPA00067; UER00123.
DR   Proteomes; UP000001168; 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..134
FT                   /note="L-ectoine synthase"
FT                   /id="PRO_0000220147"
SQ   SEQUENCE   134 AA;  15321 MW;  52B1A864E0C8A54B CRC64;
     MKVVKLADII GTNRDVDGGN WRSQRIVVES DGMGYSLHDT QIKAGTETHL WYKYHLESVY
     VIEGEGEVET VKDGKVWPVK QYECYVLDKN DEHLLRAKTD MRMVCVFNPP VTGEEVHDED
     GAYPLPEHMK PLNS