ECTC_SPHAL
ID ECTC_SPHAL Reviewed; 137 AA.
AC Q1GNW6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Sala_2951;
OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS (Sphingomonas alaskensis).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=317655;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13593 / LMG 18877 / RB2256;
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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; CP000356; ABF54656.1; -; Genomic_DNA.
DR RefSeq; WP_011543220.1; NC_008048.1.
DR PDB; 5BXX; X-ray; 2.00 A; A/B/C/D=1-137.
DR PDB; 5BY5; X-ray; 1.20 A; A=1-137.
DR PDBsum; 5BXX; -.
DR PDBsum; 5BY5; -.
DR AlphaFoldDB; Q1GNW6; -.
DR SMR; Q1GNW6; -.
DR STRING; 317655.Sala_2951; -.
DR EnsemblBacteria; ABF54656; ABF54656; Sala_2951.
DR KEGG; sal:Sala_2951; -.
DR eggNOG; COG1917; Bacteria.
DR HOGENOM; CLU_154525_0_0_5; -.
DR OMA; CVFNPPI; -.
DR OrthoDB; 1928636at2; -.
DR BRENDA; 4.2.1.108; 12995.
DR UniPathway; UPA00067; UER00123.
DR Proteomes; UP000006578; 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 1: Evidence at protein level;
KW 3D-structure; Lyase; Reference proteome.
FT CHAIN 1..137
FT /note="L-ectoine synthase"
FT /id="PRO_1000067239"
FT REGION 115..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:5BXX"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:5BY5"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:5BY5"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:5BY5"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:5BY5"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:5BY5"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:5BXX"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:5BY5"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:5BY5"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:5BY5"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:5BY5"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:5BY5"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:5BY5"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:5BY5"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5BXX"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:5BXX"
SQ SEQUENCE 137 AA; 15150 MW; F71B7E7050F34351 CRC64;
MIVRNLGDIR KTDRNVRSDG WASARMLLKD DGMGFSFHVT TLFAGSELRM HYQNHLEAVL
VLKGTGTIED LATGEVHALR PGVMYALDDH DRHIVRPETD ILTACVFNPP VTGREVHDES
GAYPADPELA REPVAAD
