ID   ECTC_BORPD              Reviewed;         133 AA.
AC   A9IJZ8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=Bpet1983;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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; AM902716; CAP42323.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9IJZ8; -.
DR   SMR; A9IJZ8; -.
DR   STRING; 94624.Bpet1983; -.
DR   EnsemblBacteria; CAP42323; CAP42323; Bpet1983.
DR   KEGG; bpt:Bpet1983; -.
DR   eggNOG; COG0662; Bacteria.
DR   OMA; CVFNPPI; -.
DR   UniPathway; UPA00067; UER00123.
DR   Proteomes; UP000001225; 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..133
FT                   /note="L-ectoine synthase"
FT                   /id="PRO_1000139967"
SQ   SEQUENCE   133 AA;  14785 MW;  80331233B61487B0 CRC64;
     MIVRNVKDVI GTQDEVRTDT WVSRRVLLKK DGMGFSFHET TIFPGGRTHI HYKNHLEAVW
     CIEGDGSIET IADGKKYELG PGVVYALNEH DEHWLCGGKE PLRVICVFNP PLTGQEVHDA
     DGVYALPAEA QAA