ECTC_BRADU
ID ECTC_BRADU Reviewed; 128 AA.
AC Q89TD1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=blr2106;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC47371.1; -; Genomic_DNA.
DR RefSeq; NP_768746.1; NC_004463.1.
DR RefSeq; WP_011084901.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89TD1; -.
DR SMR; Q89TD1; -.
DR STRING; 224911.27350360; -.
DR EnsemblBacteria; BAC47371; BAC47371; BAC47371.
DR GeneID; 64021860; -.
DR KEGG; bja:blr2106; -.
DR PATRIC; fig|224911.44.peg.1617; -.
DR eggNOG; COG0662; Bacteria.
DR HOGENOM; CLU_154525_0_0_5; -.
DR InParanoid; Q89TD1; -.
DR OMA; CVFNPPI; -.
DR PhylomeDB; Q89TD1; -.
DR UniPathway; UPA00067; UER00123.
DR Proteomes; UP000002526; 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..128
FT /note="L-ectoine synthase"
FT /id="PRO_0000220150"
SQ SEQUENCE 128 AA; 14396 MW; F094D09F439C17C9 CRC64;
MIVRSLHDIE ATDHFVDWGN STSHRLLTDK DGMGFSICHT IVRANTVSLL QYRNHLEACF
CIGGEGEVED MDGNVFPIRR GDMYVLDKHD KHLLRGGPDK DMILVSIFNP PLTGTERHKL
DDPAGSTY