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A7SN31 (MTAP_NEMVE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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=MTAPase
Gene names
ORF Names:v1g214799
OrganismNematostella vectensis (Starlet sea anemone) [Reference proteome]
Taxonomic identifier45351 [NCBI]
Taxonomic lineageEukaryotaMetazoaCnidariaAnthozoaHexacoralliaActiniariaEdwardsiidaeNematostella

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_03155

Catalytic activity

S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate. HAMAP-Rule MF_03155

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (phosphorylase route): step 1/1. HAMAP-Rule MF_03155

Subunit structure

Homotrimer By similarity. HAMAP-Rule MF_03155

Subcellular location

Cytoplasm By similarity. Nucleus By similarity HAMAP-Rule MF_03155.

Sequence similarities

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

Ontologies

Keywords
   Biological processPurine salvage
   Cellular componentCytoplasm
Nucleus
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-methionine salvage from methylthioadenosine

Inferred from electronic annotation. Source: UniProtKB-HAMAP

purine ribonucleoside salvage

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionS-methyl-5-thioadenosine phosphorylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

phosphorylase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_03155
PRO_0000415121

Regions

Region56 – 572Phosphate binding By similarity
Region89 – 902Phosphate binding By similarity
Region216 – 2183Substrate binding By similarity

Sites

Binding site141Phosphate By similarity
Binding site1921Substrate; via amide nitrogen By similarity
Binding site1931Phosphate By similarity
Site1741Important for substrate specificity By similarity
Site2291Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
A7SN31 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 4790357944AF347A

FASTA29832,721
        10         20         30         40         50         60 
MANVKVKIGI IGGTGVDNPN IMTDRQEKFV DTPFGKPSEP LITGNIQGVE CVLIARHGRK 

        70         80         90        100        110        120 
HTVMPTDINY RANVWALKEE GCTHIVVTTA CGSLTEAYRP GEIVFPDQII DRTTKRPSTF 

       130        140        150        160        170        180 
YDGQTNSPVG VCHIPMHDPY CSVTKQILAN EAQKLGIPHH ASGVNVVIEG PRFSTRAESR 

       190        200        210        220        230        240 
MFRGLGGEII SMTAMPEVAL ANEAGLCYAA IAMVTDYDCW RDDHAPVTVE SVIATFKVNV 

       250        260        270        280        290 
ANAIKILIAA IPEIAAKDWT EIINERKSQV KPPILDSTWV MFIREYRKIG SDDASKLM 

« Hide

References

[1]"Sea anemone genome reveals ancestral eumetazoan gene repertoire and genomic organization."
Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S.
Science 317:86-94(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CH2 X CH6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS469716 Genomic DNA. Translation: EDO34894.1.
RefSeqXP_001626994.1. XM_001626944.1.

3D structure databases

ProteinModelPortalA7SN31.
SMRA7SN31. Positions 6-275.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING45351.JGI214799.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaEDO34894; EDO34894; NEMVEDRAFT_v1g214799.
GeneID5506265.
KEGGnve:NEMVE_v1g214799.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228987.
KOK00772.
OMACEAQLCY.
OrthoDBEOG771270.

Enzyme and pathway databases

UniPathwayUPA00904; UER00873.

Family and domain databases

Gene3D3.40.50.1580. 1 hit.
HAMAPMF_01963. MTAP.
InterProIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERPTHR11904. PTHR11904. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMSSF53167. SSF53167. 1 hit.
TIGRFAMsTIGR01694. MTAP. 1 hit.
PROSITEPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTAP_NEMVE
AccessionPrimary (citable) accession number: A7SN31
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: October 2, 2007
Last modified: June 11, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways