Q8Y729 (MTNN_LISMO) Reviewed, UniProtKB/Swiss-Prot

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=AdoHcy nucleosidase
Short name=SAH nucleosidase
Short name=SRH nucleosidase

Gene names

Name:	mtnN
Ordered Locus Names:	lmo1494

Organism

Listeria monocytogenes

Taxonomic identifier

1639 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	233 AA.
Sequence status	Complete.
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. HAMAP MF_01684
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 Reference proteome
Gene Ontology (GO)
Biological process	L-methionine salvage from methylthioadenosine 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: EC methylthioadenosine nucleosidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 233	233	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684		PRO_0000359313
Regions
	Region	177 – 178	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	156	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	201	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8Y729 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 84E2B55219A40968	FASTA	233	25,381
	10 20 30 40 50 60 MTIGIIGAME EEVELLKNSM SSVEEIVIGG AKFYIGEIAS KEVVLLESGI GKVNAALGTT 70 80 90 100 110 120 LMADRFKPEV IINTGSAGGM AEGLAVGDVI ISDRLAYGDV DVTEFGYTYG QVPRMPAFYQ 130 140 150 160 170 180 GDAVLLKKAE TIYREYFATS ENKAVYGLVV TNDSFIMRPD QHEIIRTFFP DVKAVEMEAA 190 200 210 220 230 AIAQVAYQFD IPFLIIRAIS DLANQEATIS FDEFIHLAAK QSATCIIELL KTI

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e / Serovar 1/2a.

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Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591979 Genomic DNA. Translation: CAC99572.1.
PIR	AF1261.
RefSeq	NP_465019.1. NC_003210.1.
3D structure databases
HSSP	HSSP built from PDB template 1JYS based on UniProtKB P0AF12.
ProteinModelPortal	Q8Y729.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	986944.
GenomeReviews	Gene locus lmo1494 in contig AL591824_GR.
KEGG	lmo:lmo1494.
PATRIC	20312115. VBILisMon69206_1534.
Organism-specific databases
GenoList	LMO1494.
Phylogenomic databases
HOGENOM	HBG367723.
OMA	VIGAMEQ.
ProtClustDB	CLSK564452.
Enzyme and pathway databases
BioCyc	LMON169963:LMO1494-MONOMER.
Family and domain databases
HAMAP	MF_01684. Salvage_tnN. [Tree]
InterPro	IPR010049. MTA_SAH_Nsdase. IPR018017. Nucleoside_phosphorylase. IPR000845. Nucleoside_phosphorylase_d. [Graphical view]
KO	K01243.
PANTHER	PTHR21234. PNP_UDP. 1 hit. PTHR21234:SF6. PTHR21234:SF6. 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_LISMO

Accession

Primary (citable) accession number: Q8Y729

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program