Skip Header

Contribute Send feedback
Read comments (?) or add your own

O32028 (MTNN_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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, pfs
Ordered Locus Names:BSU27270
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length231 AA.
Sequence statusComplete.
Protein existenceInferred 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-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

Sequence similarities

Belongs to the PNP/UDP phosphorylase family. MtnN subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2312315'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP-Rule MF_01684
PRO_0000164435

Regions

Region174 – 1752Substrate binding By similarity

Sites

Active site121Proton acceptor By similarity
Binding site781Substrate; via amide nitrogen By similarity
Binding site1981Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O32028 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 7F6B8BC8EDA1E728

FASTA23125,265
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[3]"The methionine salvage pathway in Bacillus subtilis."
Sekowska A., Danchin A.
BMC Microbiol. 2:8-8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL009126 Genomic DNA. Translation: CAB14669.1.
PIRD69980.
RefSeqNP_390605.1. NC_000964.3.

3D structure databases

ProteinModelPortalO32028.
SMRO32028. Positions 1-230.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU27270.

Proteomic databases

PaxDbO32028.
PRIDEO32028.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14669; CAB14669; BSU27270.
GeneID938153.
KEGGbsu:BSU27270.
PATRIC18977310. VBIBacSub10457_2844.

Organism-specific databases

GenoListBSU27270. [Micado]

Phylogenomic databases

eggNOGCOG0775.
HOGENOMHOG000259346.
KOK01243.
OMALLVGKAK.
ProtClustDBPRK05584.

Enzyme and pathway databases

BioCycBSUB:BSU27270-MONOMER.
MetaCyc:MONOMER-1290.
UniPathwayUPA00904; UER00871.

Family and domain databases

HAMAPMF_01684. Salvage_tnN.
InterProIPR010049. MTA_SAH_Nsdase.
IPR018017. Nucleoside_phosphorylase.
IPR000845. Nucleoside_phosphorylase_d.
[Graphical view]
PANTHERPTHR21234. PTHR21234. 1 hit.
PTHR21234:SF6. PTHR21234:SF6. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01704. MTA/SAH-Nsdase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMTNN_BACSU
AccessionPrimary (citable) accession number: O32028
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families