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A9WAL0 (MTAP_CHLAA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 38. 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:Caur_3616
OrganismChloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl) [Reference proteome] [HAMAP]
Taxonomic identifier324602 [NCBI]
Taxonomic lineageBacteriaChloroflexiChloroflexalesChloroflexaceaeChloroflexus

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_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 – 288288S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000415091

Regions

Region54 – 552Phosphate binding By similarity
Region87 – 882Phosphate binding By similarity
Region210 – 2123Substrate binding By similarity

Sites

Binding site121Phosphate By similarity
Binding site1861Substrate; via amide nitrogen By similarity
Binding site1871Phosphate By similarity
Site1681Important for substrate specificity By similarity
Site2231Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
A9WAL0 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 114F997E0A557003

FASTA28831,271
        10         20         30         40         50         60 
MHSATIGVIG GSGLYAMPDL KNPEEVRLTT PFGDPSDAFI IGELEGRRVA FLPRHGRGHR 

        70         80         90        100        110        120 
LNPSEVPARA NIYAFKLLGV RALISVSAVG SLREDYAPGH AVIPDQIFDR TKGIRPATFF 

       130        140        150        160        170        180 
EGGVVAHVAF DRPFCPYLSN ILLHAAQAAG AVVHQGGTLV VMEGPQFSTK AESEENRRRG 

       190        200        210        220        230        240 
HSLIGMTALP EAKLAREAEI AYATLAMVTD YDVWHPEHDA VTAEQVIKVL SANVNLSQQI 

       250        260        270        280 
VRHAVAQIDE NFTSPAHDAL RYAIVTHPDH IPAAVKERLA PIAGRYWS 

« Hide

References

[1]"Complete genome sequence of the filamentous anoxygenic phototrophic bacterium Chloroflexus aurantiacus."
Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J., Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W., Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.
BMC Genomics 12:334-334(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29366 / DSM 635 / J-10-fl.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000909 Genomic DNA. Translation: ABY36800.1.
RefSeqYP_001637189.1. NC_010175.1.

3D structure databases

ProteinModelPortalA9WAL0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING324602.Caur_3616.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY36800; ABY36800; Caur_3616.
GeneID5825423.
KEGGcau:Caur_3616.
PATRIC21418674. VBIChlAur28763_4071.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228986.
KOK00772.
OMAMTNHTEA.
OrthoDBEOG6KHFXC.
ProtClustDBCLSK974891.

Enzyme and pathway databases

BioCycCAUR324602:GIXU-3669-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]
TIGRFAMsTIGR01694. MTAP. 1 hit.
PROSITEPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTAP_CHLAA
AccessionPrimary (citable) accession number: A9WAL0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: February 5, 2008
Last modified: February 19, 2014
This is version 38 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