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Q7VDN6 (MTAP_PROMA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Gene names
Name:mtnP
Ordered Locus Names:Pro_0332
OrganismProchlorococcus marinus (strain SARG / CCMP1375 / SS120) [Reference proteome] [HAMAP]
Taxonomic identifier167539 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length314 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_01963

Catalytic activity

S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate. HAMAP-Rule MF_01963

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_01963

Subunit structure

Homohexamer. Dimer of a homotrimer By similarity. HAMAP-Rule MF_01963

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415097

Regions

Region73 – 742Phosphate binding By similarity
Region106 – 1072Phosphate binding By similarity
Region231 – 2333Substrate binding By similarity

Sites

Binding site311Phosphate By similarity
Binding site2071Substrate; via amide nitrogen By similarity
Binding site2081Phosphate By similarity
Site1891Important for substrate specificity By similarity
Site2441Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VDN6 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 2E6812A63C762E3B

FASTA31435,041
        10         20         30         40         50         60 
MINKHFSSEE IEQDGKSCLL KNARLGVLGG SGLYSIDSIE NIKELDIETP YGKPSDSLRI 

        70         80         90        100        110        120 
GNLGGMEVVF LARHGRHHIY TPTEIPYRAN IWALRSLNVR WILSPSAVGS LQEQVRPLDM 

       130        140        150        160        170        180 
VVPDQFIDRT HQRPLTFFCD GAVAHVTMAD PFCPTLSRLL AEEGELLMPE ARQVHKGGTY 

       190        200        210        220        230        240 
LAMEGPAFST RAESQLYRSW GCKVIGMTNH TEARLAREAE IAYTSLSMVT DYDCWHEGFG 

       250        260        270        280        290        300 
NVSVDLVIEN LAANAKLASK IVEATAKRIS KLLPPSEAHT ALKNSLMTSK DKVSETTREK 

       310 
INLFTENYWG KFNK 

« Hide

References

[1]"Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a nearly minimal oxyphototrophic genome."
Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M., Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J., Tandeau de Marsac N., Weissenbach J. expand/collapse author list , Wincker P., Wolf Y.I., Hess W.R.
Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SARG / CCMP1375 / SS120.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017126 Genomic DNA. Translation: AAP99378.1.
RefSeqNP_874726.1. NC_005042.1.

3D structure databases

ProteinModelPortalQ7VDN6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167539.Pro0332.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP99378; AAP99378; Pro_0332.
GeneID1461711.
KEGGpma:Pro_0332.
PATRIC23027261. VBIProMar8617_0341.

Phylogenomic databases

KOK00772.
OMAMTNHTEA.
OrthoDBEOG6KHFXC.
ProtClustDBCLSK919168.

Enzyme and pathway databases

BioCycPMAR167539:GJN2-338-MONOMER.
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_PROMA
AccessionPrimary (citable) accession number: Q7VDN6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: October 1, 2003
Last modified: April 16, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways