Q7A5B0 (MTNN_STAAN) 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:	SA1427

Organism

Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP]

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	228 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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-Rule MF_01684
Catalytic activity	S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine. HAMAP-Rule MF_01684 S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine. HAMAP-Rule 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-Rule 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 biosynthetic process from S-adenosylmethionine Inferred from electronic annotation. Source: HAMAP L-methionine salvage from methylthioadenosine Inferred from electronic annotation. Source: UniProtKB-UniPathway 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 – 228	228	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP-Rule MF_01684		PRO_0000359371
Regions
	Region	172 – 173	2	Substrate binding By similarity
Sites
	Active site	11	1	Proton acceptor By similarity
	Binding site	77	1	Substrate; via amide nitrogen By similarity
	Binding site	151	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	196	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7A5B0 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: C756E9386E9B19DD	FASTA	228	24,534
	10 20 30 40 50 60 MIGIIGAMEE EVTILKNKLT QLSEISVAHV KFYTGILKDR EVVITQSGIG KVNAAISTTL 70 80 90 100 110 120 LINKFKPDVI INTGSAGALD ESLNVGDVLI SDDVKYHDAD ATAFGYEYGQ IPQMPVAFQS 130 140 150 160 170 180 SKPLIEKVSQ VVQQQQLTAK VGLIVSGDSF IGSVEQRQKI KKAFPNAMAV EMEATAIAQT 190 200 210 220 CYQFNVPFVV VRAVSDLANG EAEMSFEAFL EKAAVSSSQT VEALVSQL

References

[1]

"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: N315.

[2]

"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: N315.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000018 Genomic DNA. Translation: BAB42691.1.
PIR	F89941.
RefSeq	NP_374712.1. NC_002745.2.
3D structure databases
HSSP	HSSP built from PDB template 1JYS based on UniProtKB P0AF12.
ProteinModelPortal	Q7A5B0.
SMR	Q7A5B0. Positions 1-228.
ModBase	Search...
Protein-protein interaction databases
STRING	158879.SA1427.
Proteomic databases
PRIDE	Q7A5B0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB42691; BAB42691; BAB42691.
GeneID	1124269.
KEGG	sau:SA1427.
PATRIC	19575132. VBIStaAur116463_1536.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0775.
HOGENOM	HOG000259346.
KO	K01243.
OMA	SIGRHEV.
ProtClustDB	CLSK885455.
Enzyme and pathway databases
BioCyc	SAUR158879:GJCB-1498-MONOMER.
UniPathway	UPA00904; UER00871.
Family and domain databases
HAMAP	MF_01684. Salvage_tnN.
InterPro	IPR010049. MTA_SAH_Nsdase. IPR018017. Nucleoside_phosphorylase. IPR000845. Nucleoside_phosphorylase_d. [Graphical view]
PANTHER	PTHR21234. PTHR21234. 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...
Other
BindingDB	Q7A5B0.

Entry information

Entry name

MTNN_STAAN

Accession

Primary (citable) accession number: Q7A5B0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program