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Q812S1 (MTNN_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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:BC_4368
OrganismBacillus cereus (strain ATCC 14579 / DSM 31)
Taxonomic identifier226900 [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_0000359274

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
Q812S1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: EC0342DC9970CD04

FASTA23125,226
        10         20         30         40         50         60 
MRIAVIGAME EEVRILRDKL EQAETETVAG CEFTKGLLAG HEVILLKSGI GKVNAAMSTT 

        70         80         90        100        110        120 
ILLEKYKPEK VINTGSAGGF HHSLNVGDVV ISTEVRHHDV DVTAFNYEYG QVPGMPPGFK 

       130        140        150        160        170        180 
ADEALVALAE KCMQAEENIQ VVKGMIATGD SFMSDPNRVA AIRDKFENLY AVEMEAAAVA 

       190        200        210        220        230 
QVCHQYEIPF VIIRALSDIA GKESNVSFDQ FLDQAALHST NFIVKVLEEL K 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP11281.1.
RefSeqNP_834080.1. NC_004722.1.

3D structure databases

HSSPHSSP built from PDB template 1JYS based on UniProtKB P0AF12.
ProteinModelPortalQ812S1.
SMRQ812S1. Positions 1-230.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ812S1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000034574; EBBACP00000033780; EBBACG00000034565.
GeneID1206713.
GenomeReviewsGene locus BC_4368 in contig AE016877_GR.
KEGGbce:BC4368.
PATRIC32604833. VBIBacCer54481_4518.

Phylogenomic databases

eggNOGCOG0775.
GeneTreeEBGT00050000000478.
HOGENOMHBG367723.
OMAVIGAMEQ.
PhylomeDBQ812S1.
ProtClustDBPRK05584.

Enzyme and pathway databases

BioCycBCER226900:BC_4368-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_BACCR
AccessionPrimary (citable) accession number: Q812S1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 53 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