Q65GT9 (MTNN_BACLD) 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:	BLi02855, BL02020

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	231 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
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 – 231	231	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684		PRO_0000359279
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)
	Q65GT9 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 598FF54834B0DE3D	FASTA	231	25,304
	10 20 30 40 50 60 MKIAVIGAME EEVTILRSKL EQTNREVIAN CEFTSGFYEG KEVVLLKSGI GKVNAAMSTT 70 80 90 100 110 120 ILLDRFKPDV VINTGSAGGF HHSLNVGDIV ISTEVRHHDV DVTAFDYEYG QVPNLPAAYK 130 140 150 160 170 180 ADNALIQAAE DEASELGHIQ VVKGTIATGD SFMSDPDRVA FIRGKFEDLY AVEMEAAAVA 190 200 210 220 230 QVSYQFNTPF VVIRALSDIA GKESEISFDQ FLEQAAKHST DLVLRMIKRI N

References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000002 Genomic DNA. Translation: AAU24361.1. AE017333 Genomic DNA. Translation: AAU41725.1.
RefSeq	YP_079999.1. NC_006270.3. YP_092418.1. NC_006322.1.
3D structure databases
HSSP	HSSP built from PDB template 1JYS based on UniProtKB P0AF12.
ProteinModelPortal	Q65GT9.
SMR	Q65GT9. Positions 1-230.
ModBase	Search...
Protein-protein interaction databases
STRING	Q65GT9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000058191; EBBACP00000056722; EBBACG00000058182. EBBACT00000061385; EBBACP00000059818; EBBACG00000061376.
GeneID	3028537. 3098114.
GenomeReviews	Gene locus BLi02855 in contig AE017333_GR. Gene locus BL02020 in contig CP000002_GR.
KEGG	bld:BLi02855. bli:BL02020.
NMPDR	fig|279010.5.peg.3146.
PATRIC	18951422. VBIBacLic203714_2912.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0775.
GeneTree	EBGT00050000000478.
HOGENOM	HBG367723.
OMA	LEHFPTM.
PhylomeDB	Q65GT9.
ProtClustDB	PRK05584.
Enzyme and pathway databases
BioCyc	BLIC279010-1:BLI02855-MONOMER. BLIC279010:BL02020-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_BACLD

Accession

Primary (citable) accession number: Q65GT9
Secondary accession number(s): Q62S98

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program