ECTC_VIBPA
ID ECTC_VIBPA Reviewed; 128 AA.
AC Q87NZ8;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=VP1720;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(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; BA000031; BAC59983.1; -; Genomic_DNA.
DR RefSeq; NP_798099.1; NC_004603.1.
DR RefSeq; WP_005464385.1; NC_004603.1.
DR AlphaFoldDB; Q87NZ8; -.
DR SMR; Q87NZ8; -.
DR STRING; 223926.28806712; -.
DR EnsemblBacteria; BAC59983; BAC59983; BAC59983.
DR GeneID; 1189227; -.
DR KEGG; vpa:VP1720; -.
DR PATRIC; fig|223926.6.peg.1640; -.
DR eggNOG; COG0662; Bacteria.
DR HOGENOM; CLU_154525_0_0_6; -.
DR OMA; CVFNPPI; -.
DR UniPathway; UPA00067; UER00123.
DR Proteomes; UP000002493; Chromosome 1.
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_0000220160"
SQ SEQUENCE 128 AA; 14753 MW; 02734D5007CEB2C5 CRC64;
MIVRTLDECR NSERRVVADN WESVRMLLKD DNMGFSFHIT TIYEGTETHI HYQNHLESVF
CMSGEGEIEV VGGETYPIKP GTLYILDKHD EHYLRAYKNK EMVMACVFNP PITGAEVHDE
NGVYPLVD