A1A7K5 (MTNN_ECOK1) 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:	Ecok1_01510
ORF Names:	APECO1_1826

Organism

Escherichia coli O1:K1 / APEC [Complete proteome] [HAMAP]

Taxonomic identifier

405955 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	232 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-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
Subunit structure	Homodimer By similarity. 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 – 232	232	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP-Rule MF_01684		PRO_0000359298
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)
	A1A7K5 [UniParc]. Last modified January 23, 2007. 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]

"The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes." Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K. J. Bacteriol. 189:3228-3236(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000468 Genomic DNA. Translation: ABI99644.1.
RefSeq	YP_851359.1. NC_008563.1.
3D structure databases
ProteinModelPortal	A1A7K5.
SMR	A1A7K5. Positions 1-232.
ModBase	Search...
Protein-protein interaction databases
STRING	405955.APECO1_1826.
Proteomic databases
PRIDE	A1A7K5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABI99644; ABI99644; APECO1_1826.
GeneID	4495482.
KEGG	ecv:APECO1_1826.
PATRIC	18211717. VBIEscCol127180_0172.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0775.
HOGENOM	HOG000259346.
KO	K01243.
OMA	QRAGCEI.
ProtClustDB	PRK05584.
Enzyme and pathway databases
UniPathway	UPA00904; UER00871.
Family and domain databases
Gene3D	3.40.50.1580. 1 hit.
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	A1A7K5.

Entry information

Entry name

MTNN_ECOK1

Accession

Primary (citable) accession number: A1A7K5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program