ECTC_THEFY
ID ECTC_THEFY Reviewed; 134 AA.
AC Q47T77;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 106.
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=Tfu_0302;
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ54340.1; -; Genomic_DNA.
DR RefSeq; WP_011290749.1; NC_007333.1.
DR AlphaFoldDB; Q47T77; -.
DR SMR; Q47T77; -.
DR STRING; 269800.Tfu_0302; -.
DR DNASU; 3579975; -.
DR EnsemblBacteria; AAZ54340; AAZ54340; Tfu_0302.
DR KEGG; tfu:Tfu_0302; -.
DR eggNOG; COG1917; Bacteria.
DR HOGENOM; CLU_154525_0_0_11; -.
DR OMA; CVFNPPI; -.
DR OrthoDB; 1928636at2; -.
DR UniPathway; UPA00067; UER00123.
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..134
FT /note="L-ectoine synthase"
FT /id="PRO_1000067240"
SQ SEQUENCE 134 AA; 15083 MW; 634E9C8812AA09AC CRC64;
MIVRSLDDIN GTDADVVTEN WRSRRIVLAR DGVGFSFHET VLYAGTETSM WYANHIELVH
CIEGEAEVTN DETGETFLIT PGTLYLLNGH ERHTVRPKTD FRVLCVFTPP VTGREVHDEN
GSYPLLTEDA TDTD