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Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

mtnP

Organism
Synechocystis sp. (strain PCC 6803 / GT-S)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.UniRule annotation

Catalytic activityi

S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation

Pathway:iL-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 (phosphorylase route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. S-methyl-5'-thioadenosine phosphorylase (mtnP)
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 (phosphorylase route), the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei44 – 441PhosphateUniRule annotation
Sitei202 – 2021Important for substrate specificityUniRule annotation
Binding sitei220 – 2201Substrate; via amide nitrogenUniRule annotation
Binding sitei221 – 2211PhosphateUniRule annotation
Sitei257 – 2571Important for substrate specificityUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Enzyme and pathway databases

BioCyciSSP1148:GJOT-2026-MONOMER.
UniPathwayiUPA00904; UER00873.

Names & Taxonomyi

Protein namesi
Recommended name:
S-methyl-5'-thioadenosine phosphorylaseUniRule annotation (EC:2.4.2.28UniRule annotation)
Alternative name(s):
5'-methylthioadenosine phosphorylaseUniRule annotation
Short name:
MTA phosphorylaseUniRule annotation
Short name:
MTAPUniRule annotation
Gene namesi
Name:mtnPUniRule annotation
Ordered Locus Names:SYNGTS_1998
OrganismiSynechocystis sp. (strain PCC 6803 / GT-S)
Taxonomic identifieri1111707 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326S-methyl-5'-thioadenosine phosphorylasePRO_0000416437Add
BLAST

Interactioni

Subunit structurei

Homohexamer. Dimer of a homotrimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP0DJF9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni86 – 872Phosphate bindingUniRule annotation
Regioni119 – 1202Phosphate bindingUniRule annotation
Regioni244 – 2463Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.UniRule annotation

Phylogenomic databases

KOiK00772.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP.
InterProiIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01694. MTAP. 1 hit.

Sequencei

Sequence statusi: Complete.

P0DJF9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGMIISMAMT AVTIWTKTKP GRVSCFIRKN STMVNAPIGI IGGSGLYQME
60 70 80 90 100
ALKNVEEVTL DTPFGAPSDS FIVGELAGVR VAFLARHGRG HHLLPSEIPF
110 120 130 140 150
RANIHGMKQL GVKYLISASA VGSLQAEAKP LDMVVPDQFI DRTRQRISTF
160 170 180 190 200
FGEGIVAHIG FGNPICPQLA QCLSTAIAGL ELEGVTLHDR GTYVSMEGPA
210 220 230 240 250
FSTIAESNLY RSWGGTVIGM TNLPEAKLAR EAEIAYATLA LVTDYDCWHP
260 270 280 290 300
DHDHVTVEMV IGNLQKNAVN AQQVILETVK QLAANPFESI AHRALQYAVL
310 320
TPPDKFPAAT YEKLSLLLGK YYPPAP
Length:326
Mass (Da):35,319
Last modified:March 21, 2012 - v1
Checksum:i06F7D98E67A7BCD8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP012205 Genomic DNA. Translation: BAK50746.1.

Genome annotation databases

EnsemblBacteriaiBAK50746; BAK50746; SYNGTS_1998.
KEGGisyy:SYNGTS_1998.
syz:MYO_120170.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP012205 Genomic DNA. Translation: BAK50746.1.

3D structure databases

ProteinModelPortaliP0DJF9.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAK50746; BAK50746; SYNGTS_1998.
KEGGisyy:SYNGTS_1998.
syz:MYO_120170.

Phylogenomic databases

KOiK00772.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00873.
BioCyciSSP1148:GJOT-2026-MONOMER.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP.
InterProiIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01694. MTAP. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genomic structure of the cyanobacterium Synechocystis sp. PCC 6803 strain GT-S."
    Tajima N., Sato S., Maruyama F., Kaneko T., Sasaki N.V., Kurokawa K., Ohta H., Kanesaki Y., Yoshikawa H., Tabata S., Ikeuchi M., Sato N.
    DNA Res. 18:393-399(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / GT-S.

Entry informationi

Entry nameiMTAP_SYNYG
AccessioniPrimary (citable) accession number: P0DJF9
Secondary accession number(s): P74469
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: March 21, 2012
Last modified: July 22, 2015
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.