Reviewed, UniProtKB/Swiss-Prot Q5PD46 (MTNN_SALPA)

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:	SPA0213

Organism

Salmonella paratyphi A [Complete proteome] [HAMAP]

Taxonomic identifier

54388 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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 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
Subunit structure	Homodimer By similarity. 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 biosynthetic process from S-adenosylmethionine Inferred from electronic annotation. Source: HAMAP 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: 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_0000359334
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)
	Q5PD46-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 4715BDDE1A019984	FASTA	232	24,374
	10 20 30 40 50 60 MKIGIIGAME EEVTLLRDKI DNRQTITLGG CEIYTGQLNG TEVALLKSGI GKVAAALGAT 70 80 90 100 110 120 LLLGHCKPDV IINTGSAGGL ASTLKVGDIV VSDEARYHDA DVTAFGYEYG QLPGCPAGFK 130 140 150 160 170 180 ADDKLIAAAE SCIRELNLNA VRGLIVSGDA FINGSVGLAK IRHNFPDAVA VEMEATAIAH 190 200 210 220 230 VCHNFNVPFV VVRAISDVAD QQSHLSFDEF LAVAAKQSTL MVETLVQKLA HG

References

[1]

"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid." McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K. Nat. Genet. 36:1268-1274(2004) [PubMed: 15531882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000026 Genomic DNA. Translation: AAV76243.1.
RefSeq	YP_149555.1.
3D structure databases
HSSP	HSSP built from PDB template 1JYS based on UniProtKB P0AF12.
SMR	Q5PD46. Positions 1-232.
ModBase	Search...
Genome annotation databases
GeneID	3174731.
GenomeReviews	Gene locus SPA0213 in contig CP000026_GR.
KEGG	spt:SPA0213.
NMPDR	fig|295319.3.peg.83.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG367723.
OMA	NQEATIS.
Enzyme and pathway databases
BioCyc	SENT295319:SPA0213-MONOMER.
Family and domain databases
HAMAP	MF_01684. Salvage_tnN. [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_SALPA

Accession

Primary (citable) accession number: Q5PD46

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	January 4, 2005
Last modified:	February 9, 2010
This is version 33 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)