ECTC_RHOJR
ID ECTC_RHOJR Reviewed; 132 AA.
AC Q0SH55;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 100.
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};
GN OrderedLocusNames=RHA1_ro01307;
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000431; ABG93131.1; -; Genomic_DNA.
DR RefSeq; WP_009474015.1; NC_008268.1.
DR AlphaFoldDB; Q0SH55; -.
DR SMR; Q0SH55; -.
DR STRING; 101510.RHA1_ro01307; -.
DR DNASU; 4219161; -.
DR EnsemblBacteria; ABG93131; ABG93131; RHA1_ro01307.
DR KEGG; rha:RHA1_ro01307; -.
DR eggNOG; COG1917; Bacteria.
DR HOGENOM; CLU_154525_0_0_11; -.
DR OMA; CVFNPPI; -.
DR UniPathway; UPA00067; UER00123.
DR Proteomes; UP000008710; 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..132
FT /note="L-ectoine synthase"
FT /id="PRO_1000067236"
SQ SEQUENCE 132 AA; 14883 MW; 8E0DCFF2718AB5C0 CRC64;
MIVRTTAEIT DTDRDITSED GNWRSKRIIL GGDKVGFSFH ETTIKAGSVN EFHYANHVEA
VWLVEGTGKL IDLDNDKVYE LGPGSMYLLN GHERHRVEPE TEMRMLCVFN PPVTGREVHD
ENGVYPLVEV PA