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Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

SS1G_02233

Organism
Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211PhosphateUniRule annotation
Sitei180 – 1801Important for substrate specificityUniRule annotation
Binding sitei198 – 1981Substrate; via amide nitrogenUniRule annotation
Binding sitei199 – 1991PhosphateUniRule annotation
Sitei234 – 2341Important 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

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:SS1G_02233
OrganismiSclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
Taxonomic identifieri665079 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeSclerotinia
ProteomesiUP000001312: Unassembled WGS sequence

Subcellular locationi

Cytoplasm UniRule annotation. Nucleus UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 306306S-methyl-5'-thioadenosine phosphorylasePRO_0000415135Add
BLAST

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

STRINGi665079.A7EAA1.

Structurei

3D structure databases

ProteinModelPortaliA7EAA1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 642Phosphate bindingUniRule annotation
Regioni96 – 972Phosphate bindingUniRule annotation
Regioni222 – 2243Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0005.
InParanoidiA7EAA1.
KOiK00772.
OMAiHTPYGRP.
OrthoDBiEOG77DJGM.

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.

A7EAA1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVESLPTTFS DSVHIAVIGG TGLQSLEGFI PIATINPLTP WGYPSAPIHI
60 70 80 90 100
LSHNNTPIAF LSRHGTHHEL APHEIPNRAN IAALRSMGVR TIIAFSAVGS
110 120 130 140 150
LREEIKPRDF VVPDQVIDRT KGVRPFTFFE KGVVGHVGFA DPFDERIAKV
160 170 180 190 200
VRECGHALEG EGIVLHDKGT IICMEGPAFS TRAESHMYRS WGGSVINMSA
210 220 230 240 250
LPEAKLAREA EMVYQMICMA TDYDCWHSTA DVDVEMVMGH MHANGQNAKR
260 270 280 290 300
LVGAVLDALN MRWSTIDSIR RRKNKPELAN AQQHQIWRGR TYHFAWSISA

CYFSSE
Length:306
Mass (Da):33,972
Last modified:September 11, 2007 - v1
Checksum:i12F799D117340BF0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476623 Genomic DNA. Translation: EDN99379.1.
RefSeqiXP_001596017.1. XM_001595967.1.

Genome annotation databases

EnsemblFungiiEDN99379; EDN99379; SS1G_02233.
GeneIDi5492464.
KEGGissl:SS1G_02233.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476623 Genomic DNA. Translation: EDN99379.1.
RefSeqiXP_001596017.1. XM_001595967.1.

3D structure databases

ProteinModelPortaliA7EAA1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi665079.A7EAA1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEDN99379; EDN99379; SS1G_02233.
GeneIDi5492464.
KEGGissl:SS1G_02233.

Phylogenomic databases

eggNOGiCOG0005.
InParanoidiA7EAA1.
KOiK00772.
OMAiHTPYGRP.
OrthoDBiEOG77DJGM.

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. "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinerea."
    Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., Quevillon E.
    , Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.
    PLoS Genet. 7:E1002230-E1002230(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 18683 / 1980 / Ss-1.

Entry informationi

Entry nameiMTAP_SCLS1
AccessioniPrimary (citable) accession number: A7EAA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: September 11, 2007
Last modified: January 7, 2015
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.