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Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

mtnP

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 4 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.3 PublicationsUniRule annotation

Catalytic activityi

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

Kineticsi

  1. KM=147 µM for S-methyl-5'-thioadenosine1 Publication
  2. KM=109 µM for adenosine1 Publication
  3. KM=963 µM for inosine1 Publication
  4. KM=916 µM for guanosine1 Publication

pH dependencei

Optimum pH is 7.4. Active from pH 5 to 10.1 Publication

Temperature dependencei

Optimum temperature is 125 degrees Celsius. Thermostable up to 137 degrees Celsius.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101PhosphateUniRule annotation
Sitei163 – 1631Important for substrate specificityUniRule annotation
Binding sitei180 – 1801Substrate; via amide nitrogenUniRule annotation
Binding sitei181 – 1811PhosphateUniRule annotation
Sitei215 – 2151Important for substrate specificityUniRule annotation

GO - Molecular functioni

  1. phosphorylase activity Source: InterPro
  2. S-methyl-5-thioadenosine phosphorylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. L-methionine biosynthetic process from methylthioadenosine Source: UniProtKB-HAMAP
  2. purine ribonucleoside salvage Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Enzyme and pathway databases

SABIO-RKQ8U4Q8.
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
Short name:
PfMTAP
Gene namesi
Name:mtnPUniRule annotation
Ordered Locus Names:PF0016
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000001013: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 257257S-methyl-5'-thioadenosine phosphorylasePRO_0000415107Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi130 ↔ 1951 Publication
Disulfide bondi246 ↔ 2481 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ8U4Q8.

Interactioni

Subunit structurei

Homohexamer. Dimer of a homotrimer.1 PublicationUniRule annotation

Protein-protein interaction databases

STRINGi186497.PF0016.

Structurei

3D structure databases

ProteinModelPortaliQ8U4Q8.
SMRiQ8U4Q8. Positions 4-243.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 512Phosphate bindingUniRule annotation
Regioni204 – 2063Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0005.
HOGENOMiHOG000228987.
KOiK00772.
OMAiHTPYGRP.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP.
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.

Q8U4Q8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPKIGIIGGS GVYGIFEPKE TVKVHTPYGR PSAPVEIGEI EGVEVAFIPR
60 70 80 90 100
HGKYHEFPPH EVPYRANIWA LHELGVERVI AVNAVGSLKE EYKPGDIVII
110 120 130 140 150
DQFIDFTKKR EYTFYNGPRV AHISMADPFC PELRRIFIET AKELNLPVHE
160 170 180 190 200
KGTYICIEGP RFSTRAESRM FRQFADVIGM TLVPEVNLAR ELGMCYVNIS
210 220 230 240 250
TVTDYDVWAE KPVDAQEVLR VMKENEEKVQ KLLKRAIPKI PEERKCGCAD

VLKTMFV
Length:257
Mass (Da):29,220
Last modified:June 1, 2002 - v1
Checksum:iA1B8194889A30AB8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL80140.1.
RefSeqiNP_577745.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL80140; AAL80140; PF0016.
GeneIDi1467844.
KEGGipfu:PF0016.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL80140.1.
RefSeqiNP_577745.1. NC_003413.1.

3D structure databases

ProteinModelPortaliQ8U4Q8.
SMRiQ8U4Q8. Positions 4-243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF0016.

Proteomic databases

PRIDEiQ8U4Q8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL80140; AAL80140; PF0016.
GeneIDi1467844.
KEGGipfu:PF0016.

Phylogenomic databases

eggNOGiCOG0005.
HOGENOMiHOG000228987.
KOiK00772.
OMAiHTPYGRP.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00873.
SABIO-RKQ8U4Q8.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
    Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
    Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  2. "Purification and characterization of 5'-methylthioadenosine phosphorylase from the hyperthermophilic archaeon Pyrococcus furiosus: substrate specificity and primary structure analysis."
    Cacciapuoti G., Bertoldo C., Brio A., Zappia V., Porcelli M.
    Extremophiles 7:159-168(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-27, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  3. "Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and assignment of disulfide bonds."
    Cacciapuoti G., Moretti M.A., Forte S., Brio A., Camardella L., Zappia V., Porcelli M.
    Eur. J. Biochem. 271:4834-4844(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISULFIDE BONDS.
  4. "Unraveling the structural and functional differences between purine nucleoside phosphorylase and 5'-deoxy-5'-methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus."
    Cacciapuoti G., Marabotti A., Fuccio F., Porcelli M.
    Biochim. Biophys. Acta 1814:1358-1366(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiMTAP_PYRFU
AccessioniPrimary (citable) accession number: Q8U4Q8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: June 1, 2002
Last modified: January 7, 2015
This is version 69 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

Complete proteome, Direct protein sequencing, Reference proteome

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.