(data stored in ACNUC1104 zone)

SWISSPROT: ECTC_SACEN

ID   ECTC_SACEN              Reviewed;         135 AA.
AC   A4F710;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 69.
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=SACE_0485;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
CC   -!- FUNCTION: Catalyzes the circularization of gamma-N-acetyl-
CC       alpha,gamma-diaminobutyric acid (ADABA) to ectoine (1,4,5,6-
CC       tetrahydro-2-methyl-4-pyrimidine carboxylic acid), which is an
CC       excellent osmoprotectant. {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;
CC       L-ectoine from L-aspartate 4-semialdehyde: step 3/3.
CC       {ECO:0000255|HAMAP-Rule:MF_01255}.
CC   -!- SIMILARITY: Belongs to the ectoine synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01255}.
DR   EMBL; AM420293; CAL99834.1; -; Genomic_DNA.
DR   RefSeq; WP_009947387.1; NZ_PDBV01000001.1.
DR   SMR; A4F710; -.
DR   STRING; 405948.SACE_0485; -.
DR   EnsemblBacteria; CAL99834; CAL99834; SACE_0485.
DR   KEGG; sen:SACE_0485; -.
DR   eggNOG; ENOG4108Z6K; Bacteria.
DR   eggNOG; ENOG4111NEJ; LUCA.
DR   HOGENOM; HOG000078059; -.
DR   KO; K06720; -.
DR   OMA; CVFNPPI; -.
DR   OrthoDB; 1928636at2; -.
DR   BioCyc; SERY405948:SACE_RS02395-MONOMER; -.
DR   UniPathway; UPA00067; UER00123.
DR   Proteomes; UP000006728; Chromosome.
DR   GO; GO:0033990; F:ectoine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019491; P:ectoine biosynthetic process; IEA:UniProtKB-UniRule.
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   ProDom; PD080544; Ectoine_synth; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4F710.
DR   SWISS-2DPAGE; A4F710.
KW   Complete proteome; Lyase; Reference proteome.
FT   CHAIN         1    135       L-ectoine synthase.
FT                                /FTId=PRO_1000067238.
SQ   SEQUENCE   135 AA;  15387 MW;  1D3FFEE9BDDD0EDB CRC64;
     MIVRTLEEIE DTDADIKTEN WRSKRIVLAR EKVGFSVHET TLYAGTVNDF WYANHIEAVF
     VFEGEGEITD KATGETHQLK PGSLYLLNNH DKHQVRPKTD MRTVCVFNPP VTGREVHDEN
     GVYPVIVEDE EEAAS
//

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