Reviewed, UniProtKB/Swiss-Prot P0AF13 (MTNN_ECOL6)

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:	c0195

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	232 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
Subunit structure	Homodimer By similarity.
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 – 232	232	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684		PRO_0000164441
Regions
	Region	173 – 174	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	152	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	197	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0AF13-1 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: 9B1FF9BEC39D4F2C	FASTA	232	24,354
	10 20 30 40 50 60 MKIGIIGAME EEVTLLRDKI ENRQTISLGG CEIYTGQLNG TEVALLKSGI GKVAAALGAT 70 80 90 100 110 120 LLLEHCKPDV IINTGSAGGL APTLKVGDIV VSDEARYHDA DVTAFGYEYG QLPGCPAGFK 130 140 150 160 170 180 ADDKLIAAAE ACIAELNLNA VRGLIVSGDA FINGSVGLAK IRHNFPQAIA VEMEATAIAH 190 200 210 220 230 VCHNFNVPFV VVRAISDVAD QQSHLSFDEF LAVAAKQSSL MVESLVQKLA HG

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014075 Genomic DNA. Translation: AAN78689.1.
RefSeq	NP_752145.1.
3D structure databases
SMR	P0AF13. Positions 1-232.
ModBase	Search...
Genome annotation databases
GeneID	1035162.
GenomeReviews	Gene locus c0195 in contig AE014075_GR.
KEGG	ecc:c0195.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0AF13.
OMA	AQVCHQF.
Enzyme and pathway databases
BRENDA	3.2.2.9. 292881.
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_ECOL6

Accession

Primary (citable) accession number: P0AF13
Secondary accession number(s): P24247

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	November 3, 2009
This is version 27 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)