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Q7NHW1 (MTAP_GLOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 62. 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:gll2424
OrganismGloeobacter violaceus (strain PCC 7421) [Reference proteome] [HAMAP]
Taxonomic identifier251221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaGloeobacteriaGloeobacteralesGloeobacter

Protein attributes

Sequence length299 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 – 299299S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415093

Regions

Region56 – 572Phosphate binding By similarity
Region89 – 902Phosphate binding By similarity
Region215 – 2173Substrate binding By similarity

Sites

Binding site141Phosphate By similarity
Binding site1911Substrate; via amide nitrogen By similarity
Binding site1921Phosphate By similarity
Site1731Important for substrate specificity By similarity
Site2281Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NHW1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 0A134C2398AFD025

FASTA29932,753
        10         20         30         40         50         60 
MSYPQARIGV IGGSGLYQMA DLADTVEVQF NTPFGPPSDA LVIGTLAGER VAFLPRHGRG 

        70         80         90        100        110        120 
HRLLPAELPF QANIYAMKML GVEYLLSASA VGSLREEYRP RDIVFPDQFF DRTKDRPSTF 

       130        140        150        160        170        180 
FGGGLVAHIG FDQPICTELA HLAAEAARGV ELIGETRIHT GGTYVCMEGP AFSTLAESRL 

       190        200        210        220        230        240 
YRSWGMDIIG MTNLQEAKLA REAEICYATM ALVTDYDCWH PDHGAVTVEL IIDNLHKNAE 

       250        260        270        280        290 
NAQRIVRAVV ERLHAAAPPC ASHSALKYAL LTQPEDVPQA TKQKLAAILA KYPAYRPEV 

« Hide

References

[1]"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids."
Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., Tabata S.
DNA Res. 10:137-145(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7421.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000045 Genomic DNA. Translation: BAC90365.1.
RefSeqNP_925370.1. NC_005125.1.

3D structure databases

ProteinModelPortalQ7NHW1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING251221.gll2424.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC90365; BAC90365; BAC90365.
GeneID2600825.
KEGGgvi:gll2424.
PATRIC22044321. VBIGloVio86258_2461.

Phylogenomic databases

HOGENOMHOG000228986.
KOK00772.
OMACEAQLCY.
OrthoDBEOG6KHFXC.
PhylomeDBQ7NHW1.

Enzyme and pathway databases

BioCycGVIO251221:GH9A-2453-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_GLOVI
AccessionPrimary (citable) accession number: Q7NHW1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 62 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