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Protein

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase

Gene

mtnN

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine.UniRule annotation
S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine.UniRule annotation

Pathwayi: L-methionine biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (mtnN)
  2. no protein annotated in this organism
This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route), the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111Proton acceptorUniRule annotation
Binding sitei77 – 771Substrate; via amide nitrogenUniRule annotation
Binding sitei151 – 1511Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation
Active sitei196 – 1961Proton donorUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-1614-MONOMER.
BRENDAi3.2.2.16. 3352.
3.2.2.9. 3352.
UniPathwayiUPA00904; UER00871.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidaseUniRule annotation (EC:3.2.2.9UniRule annotation)
Short name:
MTA/SAH nucleosidaseUniRule annotation
Short name:
MTANUniRule annotation
Alternative name(s):
5'-methylthioadenosine nucleosidaseUniRule annotation
Short name:
MTA nucleosidaseUniRule annotation
S-adenosylhomocysteine nucleosidaseUniRule annotation
Short name:
AdoHcy nucleosidaseUniRule annotation
Short name:
SAH nucleosidaseUniRule annotation
Short name:
SRH nucleosidaseUniRule annotation
Gene namesi
Name:mtnNUniRule annotation
Ordered Locus Names:SAV1599
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000002481 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2282285'-methylthioadenosine/S-adenosylhomocysteine nucleosidasePRO_0000359369Add
BLAST

Proteomic databases

PaxDbiQ99TQ0.
PRIDEiQ99TQ0.

2D gel databases

World-2DPAGE0002:Q99TQ0.

Interactioni

Protein-protein interaction databases

STRINGi158878.SAV1599.

Structurei

Secondary structure

228
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 88Combined sources
Helixi9 – 168Combined sources
Beta strandi20 – 278Combined sources
Beta strandi30 – 378Combined sources
Beta strandi40 – 467Combined sources
Helixi51 – 6515Combined sources
Beta strandi68 – 725Combined sources
Beta strandi74 – 785Combined sources
Beta strandi88 – 9811Combined sources
Helixi102 – 1043Combined sources
Beta strandi116 – 1194Combined sources
Helixi122 – 13413Combined sources
Beta strandi139 – 1468Combined sources
Helixi154 – 16310Combined sources
Beta strandi167 – 1737Combined sources
Helixi174 – 18411Combined sources
Beta strandi188 – 1969Combined sources
Helixi202 – 22524Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BL6X-ray1.70A1-228[»]
4GMHX-ray2.00A1-228[»]
ProteinModelPortaliQ99TQ0.
SMRiQ99TQ0. Positions 1-228.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99TQ0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni172 – 1732Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DUF. Bacteria.
COG0775. LUCA.
HOGENOMiHOG000259346.
KOiK01243.
OMAiLLERCKP.
PhylomeDBiQ99TQ0.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01684. Salvage_MtnN. 1 hit.
InterProiIPR010049. MTA_SAH_Nsdase.
IPR018017. Nucleoside_phosphorylase.
IPR000845. Nucleoside_phosphorylase_d.
[Graphical view]
PANTHERiPTHR21234. PTHR21234. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01704. MTA/SAH-Nsdase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q99TQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIGIIGAMEE EVTILKNKLT QLSEISVAHV KFYTGILKDR EVVITQSGIG
60 70 80 90 100
KVNAAISTTL LINKFKPDVI INTGSAGALD ESLNVGDVLI SDDVKYHDAD
110 120 130 140 150
ATAFGYEYGQ IPQMPVAFQS SKPLIEKVSQ VVQQQQLTAK VGLIVSGDSF
160 170 180 190 200
IGSVEQRQKI KKAFPNAMAV EMEATAIAQT CYQFNVPFVV VRAVSDLANG
210 220
EAEMSFEAFL EKAAVSSSQT VEALVSQL
Length:228
Mass (Da):24,534
Last modified:June 1, 2001 - v1
Checksum:iC756E9386E9B19DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB57761.1.
RefSeqiWP_000579275.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB57761; BAB57761; SAV1599.
KEGGisav:SAV1599.
PATRICi19563938. VBIStaAur52173_1647.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB57761.1.
RefSeqiWP_000579275.1. NC_002758.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BL6X-ray1.70A1-228[»]
4GMHX-ray2.00A1-228[»]
ProteinModelPortaliQ99TQ0.
SMRiQ99TQ0. Positions 1-228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi158878.SAV1599.

2D gel databases

World-2DPAGE0002:Q99TQ0.

Proteomic databases

PaxDbiQ99TQ0.
PRIDEiQ99TQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB57761; BAB57761; SAV1599.
KEGGisav:SAV1599.
PATRICi19563938. VBIStaAur52173_1647.

Phylogenomic databases

eggNOGiENOG4105DUF. Bacteria.
COG0775. LUCA.
HOGENOMiHOG000259346.
KOiK01243.
OMAiLLERCKP.
PhylomeDBiQ99TQ0.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00871.
BioCyciSAUR158878:GJJ5-1614-MONOMER.
BRENDAi3.2.2.16. 3352.
3.2.2.9. 3352.

Miscellaneous databases

EvolutionaryTraceiQ99TQ0.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01684. Salvage_MtnN. 1 hit.
InterProiIPR010049. MTA_SAH_Nsdase.
IPR018017. Nucleoside_phosphorylase.
IPR000845. Nucleoside_phosphorylase_d.
[Graphical view]
PANTHERiPTHR21234. PTHR21234. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01704. MTA/SAH-Nsdase. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMTNN_STAAM
AccessioniPrimary (citable) accession number: Q99TQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: June 1, 2001
Last modified: September 7, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.