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Q9V2F1 (MTAP_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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:mntP
Synonyms:mtaP
Ordered Locus Names:PYRAB01230
ORF Names:PAB2264
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length257 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 – 257257S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000184560

Regions

Region50 – 512Phosphate binding By similarity
Region204 – 2063Substrate binding By similarity

Sites

Binding site101Phosphate By similarity
Binding site1801Substrate; via amide nitrogen By similarity
Binding site1811Phosphate By similarity
Site1631Important for substrate specificity By similarity
Site2151Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9V2F1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: E0C651C18B63A15C

FASTA25729,172
        10         20         30         40         50         60 
MPKIGIIGGS GVYGVFEPKE VVKIHTPYGR PSAPVEIGEI EGVEVAFIPR HGKYHEFPPH 

        70         80         90        100        110        120 
EVPYRANIWA LYELGVERII AINAVGSLKE EYKPGDIVII DQFIDFTKKR EYTFYNGPKV 

       130        140        150        160        170        180 
AHVSMADPFC PELRRIFIET AKELGLPVHE KGTYICIEGP RFSTRAESRM FRQFADVIGM 

       190        200        210        220        230        240 
TLVPEVNLAR ELGMCYVNIS TVTDYDVWAE KPVNAQEVLR VMKENEEKVQ KLLRKAIPKI 

       250 
PEERKCGCAD VLKTMFV 

« Hide

References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
Gao J., Wang J.
Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248283 Genomic DNA. Translation: CAB49047.1.
HE613800 Genomic DNA. Translation: CCE69499.1.
PIRH75199.
RefSeqNP_125816.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9V2F1.
SMRQ9V2F1. Positions 4-243.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272844.PAB2264.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB49047; CAB49047; PAB2264.
GeneID1495010.
KEGGpab:PAB2264.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228987.
KOK00772.
OMACEAQLCY.

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_PYRAB
AccessionPrimary (citable) accession number: Q9V2F1
Secondary accession number(s): G8ZFV8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 76 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