Reviewed, UniProtKB/Swiss-Prot A8FFL1 (MTNN_BACP2)

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:	BPUM_2362

Organism

Bacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]

Taxonomic identifier

315750 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	231 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
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 – 231	231	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684		PRO_0000359280
Regions
	Region	174 – 175	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	198	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8FFL1-1 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: 45C5EDB78A459A15	FASTA	231	25,232
	10 20 30 40 50 60 MKIAVIGAME EEVTILRDQL KNATQENIAG CEFTTGVYED KEVILLKSGI GKVNAAVSTT 70 80 90 100 110 120 LLLDRFQPDY VINTGSAGGF HHTLNVGDIV ISTDVRHHDV DVTIFNYEYG QVPGLPAAFV 130 140 150 160 170 180 ADEKLVKLAE ESALEIDHIQ VAKGTIATGD SFMNDPNRVA FVREKFPELY AVEMEAAAVA 190 200 210 220 230 QVCQLFGTPF VVVRALSDIA GKESNVSFDQ FLEQAAIHST DLVLRMIKQT Q

References

[1]

"Paradoxical DNA repair and peroxide resistance gene conservation in Bacillus pumilus SAFR-032." Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C. , Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., Weinstock G.M. PLoS ONE 2:E928-E928(2007) [PubMed: 17895969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000813 Genomic DNA. Translation: ABV63028.1.
RefSeq	YP_001487588.1.
3D structure databases
SMR	A8FFL1. Positions 1-229.
ModBase	Search...
Protein-protein interaction databases
STRING	A8FFL1.
Genome annotation databases
GeneID	5621631.
GenomeReviews	Gene locus BPUM_2362 in contig CP000813_GR.
KEGG	bpu:BPUM_2362.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0775.
HOGENOM	HBG367723.
OMA	TPFVIIR.
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_BACP2

Accession

Primary (citable) accession number: A8FFL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	November 13, 2007
Last modified:	February 9, 2010
This is version 17 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)