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Protein

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase

Gene

mtnN

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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 sitei12 – 121Proton acceptorUniRule annotation
Binding sitei78 – 781Substrate; via amide nitrogenUniRule annotation
Binding sitei153 – 1531Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation
Active sitei198 – 1981Proton donorUniRule annotation

GO - Molecular functioni

  • adenosylhomocysteine nucleosidase activity Source: TIGR
  • methylthioadenosine nucleosidase activity Source: TIGR

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14562.
VCHO:VC2379-MONOMER.
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:VC_2379
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000000584 Componenti: Chromosome 1

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1250374.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2312315'-methylthioadenosine/S-adenosylhomocysteine nucleosidasePRO_0000359381Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243277.VC2379.

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Helixi10 – 178Combined sources
Beta strandi21 – 288Combined sources
Beta strandi31 – 388Combined sources
Beta strandi41 – 477Combined sources
Helixi52 – 6615Combined sources
Beta strandi69 – 7911Combined sources
Beta strandi89 – 979Combined sources
Helixi103 – 1053Combined sources
Beta strandi117 – 1204Combined sources
Helixi123 – 13311Combined sources
Beta strandi141 – 1488Combined sources
Helixi156 – 16510Combined sources
Beta strandi169 – 1757Combined sources
Helixi176 – 18611Combined sources
Beta strandi190 – 1989Combined sources
Helixi204 – 22825Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DP9X-ray2.30A/C1-231[»]
ProteinModelPortaliQ9KPI8.
SMRiQ9KPI8. Positions 1-230.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9KPI8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni174 – 1752Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DUF. Bacteria.
COG0775. LUCA.
KOiK01243.
OMAiLLERCKP.
OrthoDBiEOG64JFVR.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01684. Salvage_MtnN.
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.

Q9KPI8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIGIIGAMQ QEVAILKDLI EDVQEVNQAG CTFYSGQIQG VDVVLLQSGI
60 70 80 90 100
GKVSAALGTA LLISQYAPDV VINTGSAGGF DASLNVGDVV ISSEVRHHDA
110 120 130 140 150
DVTAFGYEIG QMAGQPAAFK ADEKLMTVAE QALAQLPNTH AVRGLICTGD
160 170 180 190 200
AFVCTAERQQ FIRQHFPSVV AVEMEASAIA QTCHQFKVPF VVVRAISDVA
210 220 230
DKESPLSFEE FLPLAAKSSS AMVLKMVELL K
Length:231
Mass (Da):24,525
Last modified:October 1, 2000 - v1
Checksum:i5BEE5C1DA30A68C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF95522.1.
PIRiA82084.
RefSeqiNP_232009.1. NC_002505.1.
WP_000689868.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF95522; AAF95522; VC_2379.
GeneIDi2613048.
KEGGivch:VC2379.
PATRICi20083781. VBIVibCho83274_2265.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF95522.1.
PIRiA82084.
RefSeqiNP_232009.1. NC_002505.1.
WP_000689868.1. NC_002505.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DP9X-ray2.30A/C1-231[»]
ProteinModelPortaliQ9KPI8.
SMRiQ9KPI8. Positions 1-230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VC2379.

Chemistry

ChEMBLiCHEMBL1250374.

Protocols and materials databases

DNASUi2613048.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF95522; AAF95522; VC_2379.
GeneIDi2613048.
KEGGivch:VC2379.
PATRICi20083781. VBIVibCho83274_2265.

Phylogenomic databases

eggNOGiENOG4105DUF. Bacteria.
COG0775. LUCA.
KOiK01243.
OMAiLLERCKP.
OrthoDBiEOG64JFVR.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00871.
BioCyciMetaCyc:MONOMER-14562.
VCHO:VC2379-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9KPI8.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01684. Salvage_MtnN.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39315 / El Tor Inaba N16961.

Entry informationi

Entry nameiMTNN_VIBCH
AccessioniPrimary (citable) accession number: Q9KPI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: October 1, 2000
Last modified: December 9, 2015
This is version 90 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. 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.