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Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

FG08458.1

Organism
Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum)
Status
Unreviewed-Annotation score: -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

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 (FG08458.1)
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
Sitei179Important for substrate specificityUniRule annotation1
Binding sitei197Substrate; via amide nitrogenUniRule annotation1
Binding sitei198PhosphateUniRule annotation1
Sitei233Important for substrate specificityUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferaseUniRule annotation, Transferase
Biological processPurine salvageUniRule annotation

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
Name:FG08458.1Imported
ORF Names:FGRAMPH1_01T10007Imported
OrganismiGibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum)Imported
Taxonomic identifieri229533 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusarium
Proteomesi
  • UP000070720 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiFungiDB:FGRAMPH1_01G10007

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

CytoplasmUniRule annotation, NucleusUniRule annotation

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

STRINGi229533.XP_388634.1

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 255PNP_UDP_1InterPro annotationAdd BLAST242

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni62 – 63Phosphate bindingUniRule annotation2
Regioni95 – 96Phosphate bindingUniRule annotation2
Regioni221 – 223Substrate bindingUniRule annotation3

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili244 – 264Sequence analysisAdd BLAST21

Sequence similaritiesi

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

Keywords - Domaini

Coiled coilSequence analysis

Phylogenomic databases

eggNOGiKOG3985 Eukaryota
COG0005 LUCA
KOiK00772
OrthoDBiEOG092C46SL

Family and domain databases

HAMAPiMF_01963 MTAP, 1 hit
InterProiView protein in InterPro
IPR010044 MTAP
IPR000845 Nucleoside_phosphorylase_d
IPR035994 Nucleoside_phosphorylase_sf
IPR018099 Purine_phosphorylase-2_CS
PANTHERiPTHR42679 PTHR42679, 1 hit
PfamiView protein in Pfam
PF01048 PNP_UDP_1, 1 hit
SUPFAMiSSF53167 SSF53167, 1 hit
TIGRFAMsiTIGR01694 MTAP, 1 hit
PROSITEiView protein in PROSITE
PS01240 PNP_MTAP_2, 1 hit

Sequencei

Sequence statusi: Complete.

I1RW06-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADLPTTFDK PVHIAVIGGT GLGQLEGFEP VAALNPITPW GAPASPIQIL
60 70 80 90 100
SHKGGYVAFL ARHGVHHQFA PHEVPNRANI AALRHIGVRS IIAFSAVGSL
110 120 130 140 150
QEEIKPMDFV LPDQAIDRTK GVRPFTFFEG GVVGHVGFAD PFDAGLANVV
160 170 180 190 200
KACAAHMEGD GVVLHDKGTV VVMEGPQFST RAESHMYRSW GGSVINMSTL
210 220 230 240 250
PEAKLAREAE LAYQVIAMAT DYDCWHSFED VNVELVLKYM KANNENAKRL
260 270 280 290 300
VAGVLDRLAE LENSDLVLAK HLAGSSQGAV KFMTKPAGRN PEAMKKVEYL

FPGFWEE
Length:307
Mass (Da):33,265
Last modified:June 13, 2012 - v1
Checksum:i719B1328446CA3CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HG970333 Genomic DNA Translation: CEF76806.1
RefSeqiXP_011320310.1, XM_011322008.1

Genome annotation databases

EnsemblFungiiCEF76806; CEF76806; FGRRES_08458
GeneIDi23555462
KEGGifgr:FGSG_08458

Similar proteinsi

Entry informationi

Entry nameiI1RW06_GIBZE
AccessioniPrimary (citable) accession number: I1RW06
Entry historyiIntegrated into UniProtKB/TrEMBL: June 13, 2012
Last sequence update: June 13, 2012
Last modified: December 20, 2017
This is version 48 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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