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)DescriptionActionsGraphical viewLength
Active sitei14Proton acceptorBy similarity1
Binding sitei81Substrate; via amide nitrogen1
Binding sitei155Substrate; via amide nitrogen and carbonyl oxygen1
Active sitei199Proton donorCurated1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001644431 – 231Aminodeoxyfutalosine nucleosidaseAdd BLAST231

Proteomic databases

PaxDbiO24915.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiO24915. 2 interactors.
STRINGi85962.HP0089.

Structurei

Secondary structure

1231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Helixi12 – 22Combined sources11
Beta strandi27 – 31Combined sources5
Beta strandi34 – 41Combined sources8
Beta strandi44 – 50Combined sources7
Helixi55 – 69Combined sources15
Beta strandi72 – 82Combined sources11
Beta strandi92 – 100Combined sources9
Helixi106 – 108Combined sources3
Beta strandi120 – 123Combined sources4
Helixi126 – 139Combined sources14
Beta strandi143 – 150Combined sources8
Helixi158 – 168Combined sources11
Beta strandi171 – 176Combined sources6
Helixi177 – 187Combined sources11
Beta strandi191 – 199Combined sources9
Helixi211 – 228Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiO24915.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni175 – 176Substrate binding2

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)DescriptionActionsGraphical viewLength
Sequence conflicti25D → G in AAC64855 (Ref. 2) Curated1
Sequence conflicti109D → N in AAC64855 (Ref. 2) Curated1
Sequence conflicti134E → K in AAC64855 (Ref. 2) Curated1
Sequence conflicti142V → A in AAC64855 (Ref. 2) Curated1
Sequence conflicti147V → L in AAC64855 (Ref. 2) Curated1
Sequence conflicti230E → R in AAC64855 (Ref. 2) Curated1

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
PDB 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.
SMRiO24915.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO24915. 2 interactors.
STRINGi85962.HP0089.

Proteomic databases

PaxDbiO24915.

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: November 2, 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, 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.