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B1IQI1 (MTNN_ECOLC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 38. 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:EcolC_3500
OrganismEscherichia coli (strain ATCC 8739 / DSM 1576 / Crooks) [Complete proteome] [HAMAP]
Taxonomic identifier481805 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

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-Rule MF_01684

Catalytic activity

S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine. HAMAP-Rule MF_01684

S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine. HAMAP-Rule 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-Rule MF_01684

Subunit structure

Homodimer By similarity.

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-Rule MF_01684
PRO_0000359293

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
B1IQI1 [UniParc].

Last modified April 29, 2008. 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]"Complete sequence of Escherichia coli C str. ATCC 8739."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Ingram L., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8739 / DSM 1576 / Crooks.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000946 Genomic DNA. Translation: ACA79114.1.
RefSeqYP_001726441.1. NC_010468.1.

3D structure databases

ProteinModelPortalB1IQI1.
SMRB1IQI1. Positions 1-232.
ModBaseSearch...

Protein-protein interaction databases

STRING481805.EcolC_3500.

Proteomic databases

PRIDEB1IQI1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA79114; ACA79114; EcolC_3500.
GeneID6068499.
KEGGecl:EcolC_3500.
PATRIC18230092. VBIEscCol82905_3740.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0775.
HOGENOMHOG000259346.
KOK01243.
OMAQRAGCEI.
ProtClustDBPRK05584.

Enzyme and pathway databases

BioCycECOL481805:GI3G-3582-MONOMER.
UniPathwayUPA00904; UER00871.

Family and domain databases

HAMAPMF_01684. Salvage_tnN.
InterProIPR010049. MTA_SAH_Nsdase.
IPR018017. Nucleoside_phosphorylase.
IPR000845. Nucleoside_phosphorylase_d.
[Graphical view]
PANTHERPTHR21234. PTHR21234. 1 hit.
PTHR21234:SF6. PTHR21234:SF6. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01704. MTA/SAH-Nsdase. 1 hit.
ProtoNetSearch...

Other

BindingDBB1IQI1.

Entry information

Entry nameMTNN_ECOLC
AccessionPrimary (citable) accession number: B1IQI1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: April 29, 2008
Last modified: May 1, 2013
This is version 38 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

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