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Q99TQ0 (MTNN_STAAM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:SAV1599
OrganismStaphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]
Taxonomic identifier158878 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 – 2282285'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684
PRO_0000359369

Regions

Region172 – 1732Substrate binding By similarity

Sites

Active site111Proton acceptor By similarity
Binding site771Substrate; via amide nitrogen By similarity
Binding site1511Substrate; via amide nitrogen and carbonyl oxygen By similarity
Binding site1961Substrate By similarity

Secondary structure

1 ................................. 228
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99TQ0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: C756E9386E9B19DD

FASTA22824,534
        10         20         30         40         50         60 
MIGIIGAMEE EVTILKNKLT QLSEISVAHV KFYTGILKDR EVVITQSGIG KVNAAISTTL 

        70         80         90        100        110        120 
LINKFKPDVI INTGSAGALD ESLNVGDVLI SDDVKYHDAD ATAFGYEYGQ IPQMPVAFQS 

       130        140        150        160        170        180 
SKPLIEKVSQ VVQQQQLTAK VGLIVSGDSF IGSVEQRQKI KKAFPNAMAV EMEATAIAQT 

       190        200        210        220 
CYQFNVPFVV VRAVSDLANG EAEMSFEAFL EKAAVSSSQT VEALVSQL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000017 Genomic DNA. Translation: BAB57761.1.
RefSeqNP_372123.1. NC_002758.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BL6X-ray1.70A1-228[»]
ProteinModelPortalQ99TQ0.
SMRQ99TQ0. Positions 2-227.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ99TQ0.

2D gel databases

World-2DPAGE0002:Q99TQ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000006756; EBSTAP00000006574; EBSTAG00000006755.
GeneID1121574.
GenomeReviewsGene locus SAV1599 in contig BA000017_GR.
KEGGsav:SAV1599.
PATRIC19563938. VBIStaAur52173_1647.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0775.
GeneTreeEBGT00050000025335.
HOGENOMHBG367723.
OMALEHFPTM.
PhylomeDBQ99TQ0.
ProtClustDBCLSK885455.

Enzyme and pathway databases

BioCycSAUR158878:SAV1599-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_STAAM
AccessionPrimary (citable) accession number: Q99TQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 62 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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