Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aminodeoxyfutalosine nucleosidase

Gene

mtnN

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the direct conversion of aminodeoxyfutalosine (AFL) into dehypoxanthine futalosine (DHFL) and adenine via the hydrolysis of the N-glycosidic bond; this reaction seems to represent an essential step in the menaquinone biosynthesis pathway in Helicobacter species. Can also probably catalyzes the hydrolysis of 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. These other activities highlight the tremendous versatility of the enzyme, which also plays key roles in S-adenosylmethionine recycling and in the biosynthesis of the quorum-sensing molecule autoinducer-2. Does not act on futalosine (FL) as substrate.2 Publications

Catalytic activityi

6-amino-6-deoxyfutalosine + H2O = dehypoxanthine futalosine + adenine.2 Publications
S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine.2 Publications
S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine.2 Publications

Pathwayi: menaquinone biosynthesis

This protein is involved in the pathway menaquinone biosynthesis, which is part of Quinol/quinone metabolism.
View all proteins of this organism that are known to be involved in the pathway menaquinone biosynthesis and in Quinol/quinone metabolism.

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).
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Aminodeoxyfutalosine 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 sitei14 – 141Proton acceptorBy similarity
Binding sitei81 – 811Substrate; via amide nitrogen
Binding sitei155 – 1551Substrate; via amide nitrogen and carbonyl oxygen
Active sitei199 – 1991Proton donorCurated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Amino-acid biosynthesis, Menaquinone biosynthesis, Methionine biosynthesis

Enzyme and pathway databases

BioCyciHPY:HP0089-MONOMER.
BRENDAi3.2.2.30. 2604.
UniPathwayiUPA00079.
UPA00904; UER00871.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminodeoxyfutalosine nucleosidase (EC:3.2.2.302 Publications)
Short name:
AFL nucleosidase
Short name:
Aminofutalosine nucleosidase
Alternative name(s):
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (EC:3.2.2.92 Publications)
Short name:
MTA/SAH nucleosidase
Short name:
MTAN
6-amino-6-deoxyfutalosine N-ribosylhydrolase
Gene namesi
Name:mtnN
Synonyms:mtn
Ordered Locus Names:HP_0089
OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifieri85962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
Proteomesi
  • UP000000429 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 231231Aminodeoxyfutalosine nucleosidasePRO_0000164443Add
BLAST

Proteomic databases

PaxDbiO24915.
PRIDEiO24915.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiO24915. 2 interactions.
STRINGi85962.HP0089.

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Helixi12 – 2211Combined sources
Beta strandi27 – 315Combined sources
Beta strandi34 – 418Combined sources
Beta strandi44 – 507Combined sources
Helixi55 – 6915Combined sources
Beta strandi72 – 8211Combined sources
Beta strandi92 – 1009Combined sources
Helixi106 – 1083Combined sources
Beta strandi120 – 1234Combined sources
Helixi126 – 13914Combined sources
Beta strandi143 – 1508Combined sources
Helixi158 – 16811Combined sources
Beta strandi171 – 1766Combined sources
Helixi177 – 18711Combined sources
Beta strandi191 – 1999Combined sources
Helixi211 – 22818Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BMXX-ray1.76A/B1-231[»]
4BMYX-ray1.65A/B1-231[»]
4BMZX-ray1.79A/B1-231[»]
4BN0X-ray2.11A/B/C/D1-231[»]
ProteinModelPortaliO24915.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni175 – 1762Substrate binding

Sequence similaritiesi

Belongs to the PNP/UDP phosphorylase family.Curated

Phylogenomic databases

eggNOGiENOG4105DUF. Bacteria.
COG0775. LUCA.
KOiK18284.
OMAiSGDQFVH.

Family and domain databases

Gene3Di3.40.50.1580. 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.

O24915-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQKIGILGA MREEITPILE LFGVDFEEIP LGGNVFHKGV YHNKEIIVAY
60 70 80 90 100
SKIGKVHSTL TTTSMILAFG VQKVLFSGVA GSLVKDLKIN DLLVAIQLVQ
110 120 130 140 150
HDVDLSAFDH PLGFIPESAI FIETSESLNA LAKEVANEQH IVLKEGVIAS
160 170 180 190 200
GDQFVHSKER KEFLVSEFKA SAVEMEGASV AFVCQKFGVP CCVLRSISDN
210 220 230
ADEEANMSFD AFLEKSAQTS AKFLKSMVDE L
Length:231
Mass (Da):25,209
Last modified:January 1, 1998 - v1
Checksum:i8704A43F0189CD08
GO

Sequence cautioni

The sequence AAC64855 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251D → G in AAC64855 (Ref. 2) Curated
Sequence conflicti109 – 1091D → N in AAC64855 (Ref. 2) Curated
Sequence conflicti134 – 1341E → K in AAC64855 (Ref. 2) Curated
Sequence conflicti142 – 1421V → A in AAC64855 (Ref. 2) Curated
Sequence conflicti147 – 1471V → L in AAC64855 (Ref. 2) Curated
Sequence conflicti230 – 2301E → R in AAC64855 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD07157.1.
AF009177 Genomic DNA. Translation: AAC64855.1. Different initiation.
PIRiA64531.
RefSeqiNP_206889.1. NC_000915.1.
WP_000250146.1. NC_018939.1.

Genome annotation databases

EnsemblBacteriaiAAD07157; AAD07157; HP_0089.
GeneIDi900251.
KEGGiheo:C694_00435.
hpy:HP0089.
PATRICi20591387. VBIHelPyl33062_0094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD07157.1.
AF009177 Genomic DNA. Translation: AAC64855.1. Different initiation.
PIRiA64531.
RefSeqiNP_206889.1. NC_000915.1.
WP_000250146.1. NC_018939.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BMXX-ray1.76A/B1-231[»]
4BMYX-ray1.65A/B1-231[»]
4BMZX-ray1.79A/B1-231[»]
4BN0X-ray2.11A/B/C/D1-231[»]
ProteinModelPortaliO24915.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO24915. 2 interactions.
STRINGi85962.HP0089.

Proteomic databases

PaxDbiO24915.
PRIDEiO24915.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD07157; AAD07157; HP_0089.
GeneIDi900251.
KEGGiheo:C694_00435.
hpy:HP0089.
PATRICi20591387. VBIHelPyl33062_0094.

Phylogenomic databases

eggNOGiENOG4105DUF. Bacteria.
COG0775. LUCA.
KOiK18284.
OMAiSGDQFVH.

Enzyme and pathway databases

UniPathwayiUPA00079.
UPA00904; UER00871.
BioCyciHPY:HP0089-MONOMER.
BRENDAi3.2.2.30. 2604.

Family and domain databases

Gene3Di3.40.50.1580. 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 nameiMQMTN_HELPY
AccessioniPrimary (citable) accession number: O24915
Secondary accession number(s): O32636
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: September 7, 2016
This is version 94 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, Reference proteome

Documents

  1. Helicobacter pylori
    Helicobacter pylori (strain 26695): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.