O51931 (MTNN_BUCAP) 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
Synonyms:	mtn
Ordered Locus Names:	BUsg_204

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	235 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 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 – 235	235	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684		PRO_0000164437
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)
	O51931 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 9E10DBDE31BAF0E7	FASTA	235	26,103
	10 20 30 40 50 60 MKIGIIGAIE QEIRKIKEII NNLKIKKIGN IKIYTGTFKK IEIFLILSGI GKVSASMSTT 70 80 90 100 110 120 ISINLFQPDF IINSGSAGSL NACLKIGDII IPKKTCYYDV DLTNFGYSKG QIPEYPQTFK 130 140 150 160 170 180 TNKNLREILK EIAVEFKFKF LTGLLVTGDS FIRKSNCIKK IKNQFSSAIG VDMESTAIGQ 190 200 210 220 230 VCHNFKIPFI IIKSISDLSD NNATSHFEKN IPIASLKSSK LVKLLLKKIS SQNSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of ftsZ, the cell division gene of Buchnera aphidicola (endosymbiont of aphids) and detection of the product." Baumann L., Baumann P. Curr. Microbiol. 36:85-89(1998) [PubMed: 9425245] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF012886 Genomic DNA. Translation: AAC46071.1. AE013218 Genomic DNA. Translation: AAM67768.1.
RefSeq	NP_660557.1. NC_004061.1.
3D structure databases
ProteinModelPortal	O51931.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000000535; EBBUCP00000000535; EBBUCG00000000535.
GeneID	1005401.
GenomeReviews	Gene locus BUsg_204 in contig AE013218_GR.
KEGG	bas:BUsg204.
PATRIC	21247195. VBIBucAph100086_0211.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000008047.
HOGENOM	HBG367723.
OMA	VIGAMEQ.
ProtClustDB	CLSK315792.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG204-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_BUCAP

Accession

Primary (citable) accession number: O51931

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	June 1, 1998
Last modified:	January 25, 2012
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program