ID   ECTC_BORPA              Reviewed;         131 AA.
AC   Q7W978;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=BPP1890;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640428; CAE37191.1; -; Genomic_DNA.
DR   RefSeq; WP_003810601.1; NC_002928.3.
DR   AlphaFoldDB; Q7W978; -.
DR   SMR; Q7W978; -.
DR   EnsemblBacteria; CAE37191; CAE37191; BPP1890.
DR   GeneID; 56479328; -.
DR   GeneID; 66439335; -.
DR   KEGG; bpa:BPP1890; -.
DR   HOGENOM; CLU_154525_0_0_4; -.
DR   OMA; CVFNPPI; -.
DR   UniPathway; UPA00067; UER00123.
DR   Proteomes; UP000001421; 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.
FT   CHAIN           1..131
FT                   /note="L-ectoine synthase"
FT                   /id="PRO_0000220149"
SQ   SEQUENCE   131 AA;  14672 MW;  DED45DF1280F68C8 CRC64;
     MIVRNVKDVM GTEDEVRTDT WVSRRVLLKK DGMGFSFHET TIFPGTRTHI HYKNHLEAVW
     CIEGDGSIET IADGKTYELG PGVVYALNEN DEHWLCGGKQ PLRVICVFNP PLTGQEVHDA
     EGVYALVEEA A