Skip Header

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

S-methyl-5'-thioadenosine phosphorylase

Gene

AND_22863

Organism
Anopheles darlingi (Mosquito)
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 (AND_22863)
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 sitei15 – 151PhosphateUniRule annotation
Sitei175 – 1751Important for substrate specificityUniRule annotation
Binding sitei193 – 1931Substrate; via amide nitrogenUniRule annotation
Binding sitei194 – 1941PhosphateUniRule annotation
Sitei230 – 2301Important 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

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:
MTAPaseUniRule annotation
Gene namesi
ORF Names:AND_22863
OrganismiAnopheles darlingi (Mosquito)
Taxonomic identifieri43151 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 281281S-methyl-5'-thioadenosine phosphorylasePRO_0000415118Add
BLAST

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

STRINGi43151.ADAR001140-PA.

Structurei

3D structure databases

ProteinModelPortaliE3XFR6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 582Phosphate bindingUniRule annotation
Regioni90 – 912Phosphate bindingUniRule annotation
Regioni217 – 2193Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

InParanoidiE3XFR6.

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.

E3XFR6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWIIFSSQIG IIGGSGLDDS QIIENRTERV VNTHFGIPSD VLIEGKIAGV
60 70 80 90 100
ECVLLARHGR NHSIMPTNVN YRANIWALKT LGCTHVLVST ATGSLRDEIH
110 120 130 140 150
PGDIVIPDNF IDRTTKRVQT FYDGNELLVG VCHIPMEPAF CSRTRDVLIE
160 170 180 190 200
TARELGTAGV HNSGTVVTIE GPRFSSKAES NLFRQWGAHL VNMTLVSEVV
210 220 230 240 250
LAKEAGLCYA AIAMATDYDC WRETGEDVNV ADVLATFKKN VTKVTELIIN
260 270 280
AIPKIAALDW TETIEELAKT VNTSIMLPHS N
Length:281
Mass (Da):30,799
Last modified:February 8, 2011 - v1
Checksum:i25C4B713B9CF05E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ADMH01003944 Genomic DNA. Translation: EFR19223.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ADMH01003944 Genomic DNA. Translation: EFR19223.1.

3D structure databases

ProteinModelPortaliE3XFR6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi43151.ADAR001140-PA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

InParanoidiE3XFR6.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00873.

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

  1. "Combination of measures distinguishes pre-miRNAs from other stem-loops in the genome of the newly sequenced Anopheles darlingi."
    Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.
    BMC Genomics 11:529-529(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiMTAP_ANODA
AccessioniPrimary (citable) accession number: E3XFR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: February 8, 2011
Last modified: June 24, 2015
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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.