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Database: UniProt
Entry: A0A1B8SCG9_9MYCO
LinkDB: A0A1B8SCG9_9MYCO
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ID   A0A1B8SCG9_9MYCO        Unreviewed;       135 AA.
AC   A0A1B8SCG9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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:OBY30407.1};
GN   ORFNames=ACT18_17855 {ECO:0000313|EMBL:OBY30407.1}, BST28_19920
GN   {ECO:0000313|EMBL:ORA76909.1};
OS   Mycolicibacter kumamotonensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacter.
OX   NCBI_TaxID=354243 {ECO:0000313|EMBL:OBY30407.1, ECO:0000313|Proteomes:UP000092668};
RN   [1] {ECO:0000313|EMBL:OBY30407.1, ECO:0000313|Proteomes:UP000092668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Roo {ECO:0000313|EMBL:OBY30407.1,
RC   ECO:0000313|Proteomes:UP000092668};
RA   Greninger A.L., Cunningham G., Miller S.;
RT   "Genome sequence of Mycobacterium kumamotonense strain Roo.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ORA76909.1, ECO:0000313|Proteomes:UP000192713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45093 {ECO:0000313|EMBL:ORA76909.1,
RC   ECO:0000313|Proteomes:UP000192713};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBY30407.1}.
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DR   EMBL; LFOE01000032; OBY30407.1; -; Genomic_DNA.
DR   EMBL; MVHU01000040; ORA76909.1; -; Genomic_DNA.
DR   RefSeq; WP_019738861.1; NZ_MVHU01000040.1.
DR   AlphaFoldDB; A0A1B8SCG9; -.
DR   STRING; 354243.BST28_19920; -.
DR   PATRIC; fig|354243.3.peg.3692; -.
DR   OrthoDB; 4406415at2; -.
DR   UniPathway; UPA00067; UER00123.
DR   Proteomes; UP000092668; Unassembled WGS sequence.
DR   Proteomes; UP000192713; Unassembled WGS sequence.
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}.
SQ   SEQUENCE   135 AA;  15150 MW;  4AF54CB01DC9EDCC CRC64;
     MIVRTLAEIK GTDRDVQAKT WNSQRLLLAR DGQRFSLHET ILYAGTETSM WYANHVEAVY
     CVGGEGELTN EETGEVHPLR DGTLYLLDGH EHHRVTAHTD LRMVCVFDPP VTGQEVHDET
     GAYPLLTEET QEAAS
//
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