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Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

mtnP

Organism
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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

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 (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)DescriptionActionsGraphical viewLength
Binding sitei20PhosphateUniRule annotation1
Sitei176Important for substrate specificityUniRule annotation1
Binding sitei195Substrate; via amide nitrogenUniRule annotation1
Binding sitei196PhosphateUniRule annotation1
Sitei230Important for substrate specificityUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Enzyme and pathway databases

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:APE_1885
OrganismiAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Taxonomic identifieri272557 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum
Proteomesi
  • UP000002518 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004151021 – 275S-methyl-5'-thioadenosine phosphorylaseAdd BLAST275

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi143 ↔ 210
Disulfide bondi205 ↔ 266
Disulfide bondi264 ↔ 267

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homohexamer. Dimer of a homotrimer.UniRule annotation

Protein-protein interaction databases

STRINGi272557.APE_1885.

Structurei

Secondary structure

1275
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 7Combined sources3
Beta strandi13 – 18Combined sources6
Helixi20 – 22Combined sources3
Turni25 – 27Combined sources3
Beta strandi29 – 36Combined sources8
Beta strandi47 – 52Combined sources6
Beta strandi55 – 61Combined sources7
Turni62 – 67Combined sources6
Helixi71 – 73Combined sources3
Helixi76 – 86Combined sources11
Beta strandi90 – 101Combined sources12
Beta strandi114 – 118Combined sources5
Beta strandi130 – 132Combined sources3
Helixi144 – 157Combined sources14
Beta strandi161 – 163Combined sources3
Beta strandi166 – 170Combined sources5
Helixi178 – 186Combined sources9
Beta strandi191 – 196Combined sources6
Helixi197 – 206Combined sources10
Beta strandi210 – 219Combined sources10
Beta strandi223 – 226Combined sources4
Helixi230 – 251Combined sources22
Helixi252 – 254Combined sources3
Helixi261 – 263Combined sources3
Turni265 – 268Combined sources4
Helixi269 – 271Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WTAX-ray1.78A1-275[»]
ProteinModelPortaliQ9YAQ8.
SMRiQ9YAQ8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9YAQ8.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni62 – 63Phosphate bindingUniRule annotation2
Regioni95 – 96Phosphate bindingUniRule annotation2
Regioni219 – 221Substrate bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG01327. Archaea.
COG0005. LUCA.
HOGENOMiHOG000228987.
KOiK00772.
OMAiMTQYPEC.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP. 1 hit.
InterProiIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01694. MTAP. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9YAQ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFEITRPPGV RAHVGVIGGS GLYDPGIVEN PVEVKVSTPY GNPSDFIVVG
60 70 80 90 100
DVAGVKVAFL PRHGRGHRIP PHAINYRANI WALKALGVKW VISVSAVGSL
110 120 130 140 150
REDYRPGDFV VPDQFIDMTK NRRHYTFYDG PVTVHVSMAD PFCEDLRQRL
160 170 180 190 200
IDSGRRLGYT VHERGTYVCI EGPRFSTRAE SRVWKDVFKA DIIGMTLVPE
210 220 230 240 250
INLACEAQLC YATLAMVTDY DVWADRPVTA EEVERVMISN VERARRMLYD
260 270
VIPKLAGEPE LERCSCCRAL DTAAI
Length:275
Mass (Da):30,737
Last modified:November 1, 1999 - v1
Checksum:i86CC11C1FB2DB091
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000002 Genomic DNA. Translation: BAA80890.1.
PIRiE72575.

Genome annotation databases

EnsemblBacteriaiBAA80890; BAA80890; APE_1885.
KEGGiape:APE_1885.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000002 Genomic DNA. Translation: BAA80890.1.
PIRiE72575.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WTAX-ray1.78A1-275[»]
ProteinModelPortaliQ9YAQ8.
SMRiQ9YAQ8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272557.APE_1885.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA80890; BAA80890; APE_1885.
KEGGiape:APE_1885.

Phylogenomic databases

eggNOGiarCOG01327. Archaea.
COG0005. LUCA.
HOGENOMiHOG000228987.
KOiK00772.
OMAiMTQYPEC.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00873.

Miscellaneous databases

EvolutionaryTraceiQ9YAQ8.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP. 1 hit.
InterProiIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01694. MTAP. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMTAP_AERPE
AccessioniPrimary (citable) accession number: Q9YAQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: November 1, 1999
Last modified: November 2, 2016
This is version 92 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.