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Database: UniProt
Entry: C9YZP5_STRSW
LinkDB: C9YZP5_STRSW
Original site: C9YZP5_STRSW 
ID   C9YZP5_STRSW            Unreviewed;       132 AA.
AC   C9YZP5;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=L-ectoine synthase {ECO:0000256|ARBA:ARBA00019707, ECO:0000256|HAMAP-Rule:MF_01255};
DE            EC=4.2.1.108 {ECO:0000256|ARBA:ARBA00013192, ECO:0000256|HAMAP-Rule:MF_01255};
DE   AltName: Full=N-acetyldiaminobutyrate dehydratase {ECO:0000256|ARBA:ARBA00033271, ECO:0000256|HAMAP-Rule:MF_01255};
GN   Name=ectC {ECO:0000256|HAMAP-Rule:MF_01255,
GN   ECO:0000313|EMBL:CBG74066.1};
GN   OrderedLocusNames=SCAB_70721 {ECO:0000313|EMBL:CBG74066.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG74066.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG74066.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG74066.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
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:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000511, ECO:0000256|HAMAP-
CC         Rule:MF_01255};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC       ectoine from L-aspartate 4-semialdehyde: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00005181, ECO:0000256|HAMAP-Rule:MF_01255}.
CC   -!- SIMILARITY: Belongs to the ectoine synthase family.
CC       {ECO:0000256|ARBA:ARBA00009637, ECO:0000256|HAMAP-Rule:MF_01255}.
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DR   EMBL; FN554889; CBG74066.1; -; Genomic_DNA.
DR   RefSeq; WP_013004614.1; NC_013929.1.
DR   AlphaFoldDB; C9YZP5; -.
DR   STRING; 680198.SCAB_70721; -.
DR   GeneID; 24313120; -.
DR   KEGG; scb:SCAB_70721; -.
DR   eggNOG; COG1917; Bacteria.
DR   HOGENOM; CLU_154525_0_0_11; -.
DR   UniPathway; UPA00067; UER00123.
DR   Proteomes; UP000001444; 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; Jelly Rolls; 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; -; 1.
DR   PANTHER; PTHR39289:SF1; L-ECTOINE SYNTHASE; 1.
DR   Pfam; PF06339; Ectoine_synth; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01255};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444}.
SQ   SEQUENCE   132 AA;  14908 MW;  6CDD0E758C77AB75 CRC64;
     MIVRSFKDLE GTDRHVKAAS GTWESKRIVL AKERVGFSLH ETVLYAGTET SMWYANHVEA
     VVCVEGEAEL TDDETGRTYT ITPGTMYLLD GHERHTMRIK EDFRCLCVFN PPVTGREDHD
     ANGVYPLLTE EG
//
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