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A7GT52 (MTNN_BACCN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:Bcer98_3086
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]
Taxonomic identifier315749 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2312315'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684
PRO_0000359276

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
A7GT52 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 2F36ED21AF0AD3EC

FASTA23125,309
        10         20         30         40         50         60 
MRIAVIGAME EEVRILRDKL EQAEIESVAG CEFTKGMLVG HEVILLKSGI GKVNAAMSTT 

        70         80         90        100        110        120 
ILLERYQPEK VINTGSAGGF HHALNVGDVV ISTEVRHHDV DVTAFNYEYG QVPGMPPGFK 

       130        140        150        160        170        180 
ADKELVALAE QCMKEEENIQ VVKGMIATGD SFMSDPNRVA AIRGKFENLY AVEMEAAAVA 

       190        200        210        220        230 
QVCHQYNVPF VIIRALSDIA GKESNVSFDQ FLDQAALHST NFIVKVLKEL K 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NVH 391-98.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000764 Genomic DNA. Translation: ABS23310.1.
RefSeqYP_001376305.1. NC_009674.1.

3D structure databases

ProteinModelPortalA7GT52.
SMRA7GT52. Positions 1-230.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7GT52.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000037733; EBBACP00000036784; EBBACG00000037724.
GeneID5345627.
GenomeReviewsGene locus Bcer98_3086 in contig CP000764_GR.
KEGGbcy:Bcer98_3086.
PATRIC18934802. VBIBacCyt128034_3244.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0775.
GeneTreeEBGT00050000000478.
HOGENOMHBG367723.
OMALEHFPTM.
ProtClustDBPRK05584.

Enzyme and pathway databases

BioCycBCER315749:BCER98_3086-MONOMER.

Family and domain databases

HAMAPMF_01684. Salvage_tnN.
[Tree]
InterProIPR010049. MTA_SAH_Nsdase.
IPR018017. Nucleoside_phosphorylase.
IPR000845. Nucleoside_phosphorylase_d.
[Graphical view]
KOK01243.
PANTHERPTHR21234. PNP_UDP. 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_BACCN
AccessionPrimary (citable) accession number: A7GT52
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: September 11, 2007
Last modified: December 14, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families