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A9A3N5 (MTAP_NITMS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. 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
Gene names
Name:mtnP
Ordered Locus Names:Nmar_1401
OrganismNitrosopumilus maritimus (strain SCM1) [Reference proteome] [HAMAP]
Taxonomic identifier436308 [NCBI]
Taxonomic lineageArchaeaThaumarchaeotaNitrosopumilalesNitrosopumilaceaeNitrosopumilus

Protein attributes

Sequence length263 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 – 263263S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415105

Regions

Region55 – 562Phosphate binding By similarity
Region88 – 892Phosphate binding By similarity
Region210 – 2123Substrate binding By similarity

Sites

Binding site131Phosphate By similarity
Binding site1861Substrate; via amide nitrogen By similarity
Binding site1871Phosphate By similarity
Site1681Important for substrate specificity By similarity
Site2211Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
A9A3N5 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: F42286B331B3BFF9

FASTA26329,043
        10         20         30         40         50         60 
MEKDVEIGIF GGTGIYDSGL LEDAKEVDID TPYGKPSDTI TVGTFKGRKI AFLPRHGKKH 

        70         80         90        100        110        120 
TIPPHMINFK ANIWAFKELG VTRIIAPSAV GSLKEELAPG HFVLPTQFLD FTKSRDGSFS 

       130        140        150        160        170        180 
EDGRVIHISV ADPFCPELQS SITEVTDSLD MNIHKDCTYV CIEGPRFSTK AESKFYRTTG 

       190        200        210        220        230        240 
ADIIGMTLVP ECQLAREAQI CYASISTVTD YDVWAEKPVT AKEVLETLSK NVEGTKKILT 

       250        260 
ELIEKIPKDR SCSCAKALEE AEF 

« Hide

References

[1]"Complete sequence of Nitrosopumilus maritimus SCM1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Stahl D., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SCM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000866 Genomic DNA. Translation: ABX13297.1.
RefSeqYP_001582735.1. NC_010085.1.

3D structure databases

ProteinModelPortalA9A3N5.
SMRA9A3N5. Positions 3-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING436308.Nmar_1401.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX13297; ABX13297; Nmar_1401.
GeneID5773440.
KEGGnmr:Nmar_1401.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228986.
KOK00772.
OMACEAQLCY.

Enzyme and pathway databases

BioCycNMAR436308:GI3J-1436-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_NITMS
AccessionPrimary (citable) accession number: A9A3N5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: January 15, 2008
Last modified: May 14, 2014
This is version 40 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