SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q97W94

- MTAP_SULSO

UniProt

Q97W94 - MTAP_SULSO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
S-methyl-5'-thioadenosine phosphorylase
Gene
mtnP, SSO2343
Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
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.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=0.7 mM for S-methyl-5'-thioadenosine1 Publication
  2. KM=270 µM for adenosine

Temperature dependencei

Optimum temperature is 120 degrees Celsius. Highly thermostable.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei16 – 161Phosphate By similarity
Sitei171 – 1711Important for substrate specificity By similarity
Binding sitei190 – 1901Substrate; via amide nitrogen By similarity
Binding sitei191 – 1911Phosphate By similarity
Sitei225 – 2251Important for substrate specificity By similarity

GO - Molecular functioni

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

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

BioCyciSSOL273057:GCH2-2180-MONOMER.
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:
MTAPII
Gene namesi
Name:mtnP
Ordered Locus Names:SSO2343
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001974: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi259 – 2591C → S: Reduces thermostability of the enzyme; when associated with S-261. 1 Publication
Mutagenesisi261 – 2611C → S: Reduces thermostability of the enzyme; when associated with S-259. 1 Publication
Mutagenesisi262 – 2621C → S: Reduces thermostability of the enzyme. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 270270S-methyl-5'-thioadenosine phosphorylaseUniRule annotation
PRO_0000415109Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi138 ↔ 2051 Publication
Disulfide bondi200 ↔ 2621 Publication
Disulfide bondi259 ↔ 2611 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homohexamer. Dimer of a homotrimer.1 Publication

Protein-protein interaction databases

STRINGi273057.SSO2343.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 146
Beta strandi25 – 306
Beta strandi43 – 486
Beta strandi51 – 577
Turni58 – 603
Helixi61 – 633
Helixi67 – 693
Helixi72 – 8110
Beta strandi86 – 9712
Beta strandi110 – 1145
Beta strandi125 – 1273
Helixi139 – 15214
Beta strandi156 – 1583
Beta strandi161 – 1655
Helixi173 – 1819
Beta strandi187 – 1915
Helixi192 – 20110
Beta strandi205 – 21410
Beta strandi218 – 2214
Helixi225 – 23410
Helixi236 – 24914
Helixi256 – 2583
Turni260 – 2634
Helixi266 – 2683

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A8YX-ray1.45A/B/C/D/E/F/G/H/I/J/K/L1-270[»]
3T94X-ray1.45A/B/C/D/E/F1-270[»]
ProteinModelPortaliQ97W94.
SMRiQ97W94. Positions 1-270.

Miscellaneous databases

EvolutionaryTraceiQ97W94.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 592Phosphate binding By similarity
Regioni91 – 922Phosphate binding By similarity
Regioni214 – 2163Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0005.
HOGENOMiHOG000228986.
KOiK00772.
OMAiCEAQLCY.

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.

Q97W94-1 [UniParc]FASTAAdd to Basket

« Hide

MIEQNEKASI GIIGGSGLYD PGIFSESKEI KVYTPYGQPS DFITIGKIGN    50
KSVAFLPRHG RGHRIPPHKI NYRANIWALK ELGVRWVISV SAVGSLRMDY 100
KLGDFVIPDQ FIDMTKNREY SFFDGPVVAH VSMADPFCNS LRKLAIETAK 150
ELNIKTHESG TYICIEGPRF STRAESRTWR EVYKADIIGM TLVPEVNLAC 200
EAQMCYATIA MVTDYDVFAE IPVTAEEVTR VMAENTEKAK KLLYALIQKL 250
PEKPEEGSCS CCNSLKTALV 270
Length:270
Mass (Da):30,141
Last modified:October 1, 2001 - v1
Checksum:i682A166698935A88
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006641 Genomic DNA. Translation: AAK42494.1.
PIRiG90404.
RefSeqiNP_343704.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK42494; AAK42494; SSO2343.
GeneIDi1453821.
KEGGisso:SSO2343.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006641 Genomic DNA. Translation: AAK42494.1 .
PIRi G90404.
RefSeqi NP_343704.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2A8Y X-ray 1.45 A/B/C/D/E/F/G/H/I/J/K/L 1-270 [» ]
3T94 X-ray 1.45 A/B/C/D/E/F 1-270 [» ]
ProteinModelPortali Q97W94.
SMRi Q97W94. Positions 1-270.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 273057.SSO2343.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK42494 ; AAK42494 ; SSO2343 .
GeneIDi 1453821.
KEGGi sso:SSO2343.

Phylogenomic databases

eggNOGi COG0005.
HOGENOMi HOG000228986.
KOi K00772.
OMAi CEAQLCY.

Enzyme and pathway databases

UniPathwayi UPA00904 ; UER00873 .
BioCyci SSOL273057:GCH2-2180-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q97W94.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  2. "A novel hyperthermostable 5'-deoxy-5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus."
    Cacciapuoti G., Forte S., Moretti M.A., Brio A., Zappia V., Porcelli M.
    FEBS J. 272:1886-1899(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-259; CYS-261 AND CYS-262, SUBUNIT.
  3. "The crystal structure of 5'-deoxy-5'-methylthioadenosine phosphorylase II from Sulfolobus solfataricus, a thermophilic enzyme stabilized by intramolecular disulfide bonds."
    Zhang Y., Porcelli M., Cacciapuoti G., Ealick S.E.
    J. Mol. Biol. 357:252-262(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, DISULFIDE BONDS.

Entry informationi

Entry nameiMTAP_SULSO
AccessioniPrimary (citable) accession number: Q97W94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: October 1, 2001
Last modified: May 14, 2014
This is version 68 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

External Data

Dasty 3

Similar proteinsi