ID   ECTC_ALIF1              Reviewed;         128 AA.
AC   Q5DYF2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=VF_A1124;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000021; AAW88194.1; -; Genomic_DNA.
DR   RefSeq; WP_005423821.1; NC_006841.2.
DR   RefSeq; YP_207082.1; NC_006841.2.
DR   AlphaFoldDB; Q5DYF2; -.
DR   SMR; Q5DYF2; -.
DR   STRING; 312309.VF_A1124; -.
DR   EnsemblBacteria; AAW88194; AAW88194; VF_A1124.
DR   KEGG; vfi:VF_A1124; -.
DR   PATRIC; fig|312309.11.peg.3724; -.
DR   eggNOG; COG0662; Bacteria.
DR   HOGENOM; CLU_154525_0_0_6; -.
DR   OMA; CVFNPPI; -.
DR   OrthoDB; 1928636at2; -.
DR   UniPathway; UPA00067; UER00123.
DR   Proteomes; UP000000537; Chromosome II.
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..128
FT                   /note="L-ectoine synthase"
FT                   /id="PRO_1000067241"
SQ   SEQUENCE   128 AA;  14816 MW;  8D3C45B9C55BBAD4 CRC64;
     MIVRTLDECR DSERRVASET WESVRMLLKN DNMGFSFHIT TIYQDTETHI HYKNHLESVY
     CMSGEGEIEV VGGETYPIKP GTLYILDKHD EHYLRAYKDK EMVMACVFNP PITGAEVHDE
     NGVYPVLD