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Reviewed, UniProtKB/Swiss-Prot A7ZHQ1 (MTNN_ECO24)

Last modified February 9, 2010. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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=SAH nucleosidase
      Short name=AdoHcy nucleosidase
      Short name=SRH nucleosidase
Gene names
Name: mtnN
Ordered Locus Names: EcE24377A_0164
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length232 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

Subunit structure

Homodimer By similarity. 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 – 2322325'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684
PRO_0000359297

Regions

Region173 – 1742Substrate binding By similarity

Sites

Active site121Proton acceptor By similarity
Binding site781Substrate; via amide nitrogen By similarity
Binding site1521Substrate; via amide nitrogen and carbonyl oxygen By similarity
Binding site1971Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZHQ1-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 9B1FF9BEC39D4F2C

FASTA23224,354
        10         20         30         40         50         60 
MKIGIIGAME EEVTLLRDKI ENRQTISLGG CEIYTGQLNG TEVALLKSGI GKVAAALGAT 

        70         80         90        100        110        120 
LLLEHCKPDV IINTGSAGGL APTLKVGDIV VSDEARYHDA DVTAFGYEYG QLPGCPAGFK 

       130        140        150        160        170        180 
ADDKLIAAAE ACIAELNLNA VRGLIVSGDA FINGSVGLAK IRHNFPQAIA VEMEATAIAH 

       190        200        210        220        230 
VCHNFNVPFV VVRAISDVAD QQSHLSFDEF LAVAAKQSSL MVESLVQKLA HG 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV20698.1.
RefSeqYP_001461330.1.

3D structure databases

SMRA7ZHQ1. Positions 1-232.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZHQ1.

Genome annotation databases

GeneID5590428.
GenomeReviewsGene locus EcE24377A_0164 in contig CP000800_GR.
KEGGecw:EcE24377A_0164.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0775.
HOGENOMHBG367723.
OMANQEATIS.

Family and domain databases

HAMAPMF_01684. Salvage_tnN.
[Tree]
InterProIPR010049. MTA_SAH_Nsdase.
IPR000845. Nucleoside_phosphorylase.
IPR018017. Nucleoside_phosphorylase_1.
[Graphical view]
PANTHERPTHR21234. PNP_UDP. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01704. MTA/SAH-Nsdase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMTNN_ECO24
AccessionPrimary (citable) accession number: A7ZHQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: October 23, 2007
Last modified: February 9, 2010
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents