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Q09438 (MTAP_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:B0228.7
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length288 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-UniPathway

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-EC

phosphorylase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 288288S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_03155
PRO_0000184547

Regions

Region52 – 532Phosphate binding By similarity
Region85 – 862Phosphate binding By similarity
Region212 – 2143Substrate binding By similarity

Sites

Binding site101Phosphate By similarity
Binding site1881Substrate; via amide nitrogen By similarity
Binding site1891Phosphate By similarity
Site1701Important for substrate specificity By similarity
Site2241Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q09438 [UniParc].

Last modified February 2, 2004. Version 2.
Checksum: A998E73C52DA1D3C

FASTA28831,564
        10         20         30         40         50         60 
MVKVGIIGGS GLEDPNILLD PVTVAVDTPY GKPSDDVVEG TINGVECVLL ARHGRKHDIM 

        70         80         90        100        110        120 
PGNVNFRANL WALYSRGVDV IIASTACGSL QENVEPGHLL FPDSVFDRTT GRQSTFFDGS 

       130        140        150        160        170        180 
YDQAPGVCHI QAHPTYNEKL RQVLISTAER CQLVHHRTGF GVCIEGPRFS TKAESMVFKS 

       190        200        210        220        230        240 
WGASLVNMTM MPECILAKEL GIPYATTALV TDYDCWKEED HVTASSVMKV FAANVEKAKT 

       250        260        270        280 
LFVEAVGEIG KIDWSAEILK LKTEARESVM ISPDVVIPFL TTDNQKKF 

« Hide

References

[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FO080130 Genomic DNA. Translation: CCD61451.1.
PIRT29047.
RefSeqNP_495629.2. NM_063228.6.
UniGeneCel.16075.

3D structure databases

ProteinModelPortalQ09438.
SMRQ09438. Positions 1-287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6239.B0228.7.2.

Proteomic databases

PaxDbQ09438.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaB0228.7.1; B0228.7.1; B0228.7.
B0228.7.2; B0228.7.2; B0228.7.
GeneID174252.
KEGGcel:CELE_B0228.7.
UCSCB0228.7.1. c. elegans.

Organism-specific databases

CTD174252.
WormBaseB0228.7; CE34630; WBGene00015064.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228987.
InParanoidQ09438.
KOK00772.
OMAMTNHTEA.
PhylomeDBQ09438.

Enzyme and pathway databases

SignaLinkQ09438.
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...

Other

NextBio883235.
PROQ09438.

Entry information

Entry nameMTAP_CAEEL
AccessionPrimary (citable) accession number: Q09438
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: February 2, 2004
Last modified: April 16, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase