Reviewed, UniProtKB/Swiss-Prot O32028 (MTNN_BACSU)

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
Synonyms:	mtn, pfs
Ordered Locus Names:	BSU27270

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	231 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. Ref.2
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	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 – 231	231	5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684		PRO_0000164435
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)
	O32028-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 7F6B8BC8EDA1E728	FASTA	231	25,265
	10 20 30 40 50 60 MRLAVIGAME EEVTILRNKL ENAKTETIAH CEFTTGEYEG TEVILLKSGI GKVNAAISTT 70 80 90 100 110 120 LLLDRYKPDY VINTGSAGGF HHTLNVGDVV ISTDVRHHDV DVTAFDYEYG QVPGLPAAYA 130 140 150 160 170 180 ADEKLISITE EAVSELDGIQ VAKGTIATGD SFMNDPKRVE EVRARFSDLY AVEMEAAAVA 190 200 210 220 230 QVCHQFKTPF VVIRALSDIA GKESHVSFDQ FLEQAAVHST ELVLKVIKRI H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[2]	"Identification of yrrU as the methylthioadenosine nucleosidase gene in Bacillus subtilis." Sekowska A., Danchin A. DNA Res. 6:255-264(1999) [PubMed: 10574451] [Abstract] Cited for: FUNCTION.
[3]	"The methionine salvage pathway in Bacillus subtilis." Sekowska A., Danchin A. BMC Microbiol. 2:8-8(2002) [PubMed: 12022921] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL009126 Genomic DNA. Translation: CAB14669.1.
PIR	D69980.
RefSeq	NP_390605.1.
3D structure databases
HSSP	HSSP built from PDB template 1JYS based on UniProtKB P24247.
ModBase	Search...
Genome annotation databases
GeneID	938153.
GenomeReviews	Gene locus BSU27270 in contig AL009126_GR.
KEGG	bsu:BSU27270.
NMPDR	fig|224308.1.peg.2730.
Organism-specific databases
SubtiList	BG13800. mtnN. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	O32028.
OMA	AQVCHQF.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU2723-MON. MetaCyc:MON-1290.
BRENDA	3.2.2.9. 150.
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_BACSU

Accession

Primary (citable) accession number: O32028

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 62 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)