Reviewed, UniProtKB/Swiss-Prot A0RIY7 (MTNN_BACAH)

Names and origin

Protein names

Recommended name:
    5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
      Short name=MTA/SAH nucleosidase
      Short name=MTAN
    EC=3.2.2.9
Alternative name(s):
    5'-methylthioadenosine nucleosidase
      Short name=MTA nucleosidase
    S-adenosylhomocysteine nucleosidase
      Short name=SAH nucleosidase
      Short name=AdoHcy nucleosidase
      Short name=SRH nucleosidase

Gene names

Name:	mtnN
Ordered Locus Names:	BALH_3959

Organism

Bacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP]

Taxonomic identifier

412694 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	231 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	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 By similarity.
Catalytic activity	S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine. HAMAP MF_01684 S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine. HAMAP MF_01684
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. HAMAP MF_01684
Sequence similarities	Belongs to the PNP/UDP phosphorylase family. MtnN subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	methionine biosynthetic process from S-adenosylmethionine Inferred from electronic annotation. Source: HAMAP methionine salvage Inferred from electronic annotation. Source: InterPro nucleoside catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	adenosylhomocysteine nucleosidase activity Inferred from electronic annotation. Source: HAMAP methylthioadenosine nucleosidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 231	231	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684		PRO_0000359281
Regions
	Region	174 – 175	2	Substrate binding By similarity
Sites
	Active site	12	1	Proton acceptor By similarity
	Binding site	78	1	Substrate; via amide nitrogen By similarity
	Binding site	198	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0RIY7-1 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: 11F3ACE054DE48AC	FASTA	231	25,255
	10 20 30 40 50 60 MRIAVIGAME EEVRILRDKL EQAETETVAG CEFTKGQLAG HEVILLKSGI GKVNAAMSTT 70 80 90 100 110 120 ILLERYKPEK VINTGSAGGF HHSLNVGDVV ISTEVRHHDV DVTAFNYEYG QVPGMPPGFK 130 140 150 160 170 180 ADEALVALAE KCMQAEENIQ VVKGMIATGD SFMSDPNRVA AIRDKFENLY AVEMEAAAVA 190 200 210 220 230 QVCHQYEVPF VIIRALSDIA GKESNVSFDQ FLDQAALHST NFIVKVLEEL K

References

[1]

"The complete genome sequence of Bacillus thuringiensis Al Hakam." Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Green L.D., Han C.S. , Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S. J. Bacteriol. 189:3680-3681(2007) [PubMed: 17337577] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000485 Genomic DNA. Translation: ABK87180.1.
RefSeq	YP_896687.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A0RIY7.
Genome annotation databases
GeneID	4544591.
GenomeReviews	Gene locus BALH_3959 in contig CP000485_GR.
KEGG	btl:BALH_3959.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	AQVCHQF.
Family and domain databases
HAMAP	MF_01684. [Tree]
InterPro	IPR010049. MTA_SAH_Nsdase. IPR000845. Nucleoside_phosphorylase. IPR018017. Nucleoside_phosphorylase_1. [Graphical view]
PANTHER	PTHR21234. PNP_UDP. 1 hit.
Pfam	PF01048. PNP_UDP_1. 1 hit. [Graphical view]
TIGRFAMs	TIGR01704. MTA/SAH-Nsdase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MTNN_BACAH

Accession

Primary (citable) accession number: A0RIY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	January 9, 2007
Last modified:	November 3, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)