Part:BBa_K1981007

mtn

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase. Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Can also use 5'-isobutylthioadenosine, 5'-n-butylthioadenosine, S-adenosyl-D-homocysteine, decarboxylated adenosylhomocysteine, deaminated adenosylhomocysteine and S-2-aza-adenosylhomocysteine as substrates.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
INCOMPATIBLE WITH RFC[25]
Illegal AgeI site found at 475
1000
COMPATIBLE WITH RFC[1000]

Usage and Biology

The AI-2 “supplier” was constructed by overexpressing the mtn gene.

This part was originated from Escherichia coli strain K12.

Characterization

Protein-Data Table

Protein data table for BioBrick BBa_ automatically created by the BioBrick-AutoAnnotator version 1.0

Nucleotide sequence in RFC 10: (underlined part encodes the protein)
ATGAAAATC ... GCACATGGCTAA
ORF from nucleotide position 1 to 696 (excluding stop-codon)

Amino acid sequence: (RFC 25 scars in shown in bold, other sequence features underlined; both given below)

1
101
201

MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDA
DVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVAD
QQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG*

Sequence features: (with their position in the amino acid sequence, see the list of supported features)

RFC25 scar (shown in bold):

35 to 36

Amino acid composition:

Ala (A)	32 (13.8%)
Arg (R)	6 (2.6%)
Asn (N)	9 (3.9%)
Asp (D)	12 (5.2%)

Cys (C)	5 (2.2%)
Gln (Q)	8 (3.4%)
Glu (E)	15 (6.5%)
Gly (G)	22 (9.5%)

His (H)	7 (3.0%)
Ile (I)	18 (7.8%)
Leu (L)	23 (9.9%)
Lys (K)	11 (4.7%)

Met (M)	4 (1.7%)
Phe (F)	8 (3.4%)
Pro (P)	6 (2.6%)
Ser (S)	12 (5.2%)

Thr (T)	9 (3.9%)
Trp (W)	0 (0.0%)
Tyr (Y)	4 (1.7%)
Val (V)	21 (9.1%)

Amino acid counting

	Total number:	232
	Positively charged (Arg+Lys):	17 (7.3%)
	Negatively charged (Asp+Glu):	27 (11.6%)
	Aromatic (Phe+His+Try+Tyr):	19 (8.2%)

Biochemical parameters

	Atomic composition:	C₁₀₇₉H₁₇₃₈N₂₉₂O₃₂₉S₉
	Molecular mass [Da]:	24354.0
	Theoretical pI:	5.09
	Extinction coefficient at 280 nm [M^-1 cm^-1]:	5960 / 6273 (all Cys red/ox)

Plot for hydrophobicity, charge, predicted secondary structure, solvent accessability, transmembrane helices and disulfid bridges

Codon usage

	Organism:	E. coli	B. subtilis	S. cerevisiae	A. thaliana	P. patens	Mammals
	Codon quality (CAI):	excellent (0.82)	excellent (0.81)	good (0.63)	good (0.68)	good (0.80)	good (0.70)

Alignments (obtained from PredictProtein.org)
There were no alignments for this protein in the data base. The BLAST search was initialized and should be ready in a few hours.

Predictions (obtained from PredictProtein.org)

Subcellular Localization (reliability in brackets)

	Archaea:	-
	Bacteria:	-
	Eukarya:	-

Gene Ontology (reliability in brackets)

	Molecular Function Ontology:	0005515 0. (NaN%), 0004731 0. (NaN%)
	Biological Process Ontology:	0009164 0. (NaN%), 0009086 0. (NaN%)

Predicted features:

	Disulfid bridges:	-
	Transmembrane helices:	-

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