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Q8U4Q8

- MTAP_PYRFU

UniProt

Q8U4Q8 - MTAP_PYRFU

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Protein

S-methyl-5'-thioadenosine phosphorylase

Gene
mtnP, PF0016
Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed - Annotation score: 5 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 Publications

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 adenosine
  3. KM=963 µM for inosine
  4. KM=916 µM for guanosine

pH dependencei

Optimum pH is 7.4. Active from pH 5 to 10.

Temperature dependencei

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Phosphate By similarity
Sitei163 – 1631Important for substrate specificity By similarity
Binding sitei180 – 1801Substrate; via amide nitrogen By similarity
Binding sitei181 – 1811Phosphate By similarity
Sitei215 – 2151Important for substrate specificity By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. L-methionine salvage 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 phosphorylase (EC:2.4.2.28)
Alternative name(s):
5'-methylthioadenosine phosphorylase
Short name:
MTA phosphorylase
Short name:
MTAP
Short name:
PfMTAP
Gene namesi
Name:mtnP
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 phosphorylaseUniRule annotationPRO_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 Publication

Protein-protein interaction databases

STRINGi186497.PF0016.

Structurei

3D structure databases

ProteinModelPortaliQ8U4Q8.
SMRiQ8U4Q8. Positions 4-243.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 512Phosphate binding By similarity
Regioni204 – 2063Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0005.
HOGENOMiHOG000228987.
KOiK00772.
OMAiDYTFYNG.

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

MPKIGIIGGS GVYGIFEPKE TVKVHTPYGR PSAPVEIGEI EGVEVAFIPR    50
HGKYHEFPPH EVPYRANIWA LHELGVERVI AVNAVGSLKE EYKPGDIVII 100
DQFIDFTKKR EYTFYNGPRV AHISMADPFC PELRRIFIET AKELNLPVHE 150
KGTYICIEGP RFSTRAESRM FRQFADVIGM TLVPEVNLAR ELGMCYVNIS 200
TVTDYDVWAE KPVDAQEVLR VMKENEEKVQ KLLKRAIPKI PEERKCGCAD 250
VLKTMFV 257
Length:257
Mass (Da):29,220
Last modified:June 1, 2002 - v1
Checksum:iA1B8194889A30AB8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE009950 Genomic DNA. Translation: AAL80140.1 .
RefSeqi NP_577745.1. NC_003413.1.

3D structure databases

ProteinModelPortali Q8U4Q8.
SMRi Q8U4Q8. Positions 4-243.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 186497.PF0016.

Proteomic databases

PRIDEi Q8U4Q8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL80140 ; AAL80140 ; PF0016 .
GeneIDi 1467844.
KEGGi pfu:PF0016.

Phylogenomic databases

eggNOGi COG0005.
HOGENOMi HOG000228987.
KOi K00772.
OMAi DYTFYNG.

Enzyme and pathway databases

UniPathwayi UPA00904 ; UER00873 .
SABIO-RK Q8U4Q8.

Family and domain databases

Gene3Di 3.40.50.1580. 1 hit.
HAMAPi MF_01963. MTAP.
InterProi IPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view ]
PANTHERi PTHR11904. PTHR11904. 1 hit.
Pfami PF01048. PNP_UDP_1. 1 hit.
[Graphical view ]
SUPFAMi SSF53167. SSF53167. 1 hit.
TIGRFAMsi TIGR01694. MTAP. 1 hit.
PROSITEi PS01240. PNP_MTAP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: May 14, 2014
This is version 66 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

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