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D1YZM1 (D1YZM1_METPS) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
EC=2.4.2.28 HAMAP-Rule MF_01963
Alternative name(s):
5'-methylthioadenosine phosphorylase HAMAP-Rule MF_01963
Gene names
Name:mtnP HAMAP-Rule MF_01963
Ordered Locus Names:MCP_1821
OrganismMethanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 / SANAE) [Complete proteome] [HAMAP] EMBL BAI61893.1
Taxonomic identifier304371 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanomicrobia › Methanocellales › Methanocellaceae › Methanocella ›

Protein attributes

Sequence length281 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. HAMAP-Rule MF_01963

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region52 – 532Phosphate binding By similarity HAMAP-Rule MF_01963
Region85 – 862Phosphate binding By similarity HAMAP-Rule MF_01963
Region206 – 2083Substrate binding By similarity HAMAP-Rule MF_01963

Sites

Binding site101Phosphate By similarity HAMAP-Rule MF_01963
Binding site1821Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01963
Binding site1831Phosphate By similarity HAMAP-Rule MF_01963
Site1641Important for substrate specificity By similarity HAMAP-Rule MF_01963
Site2171Important for substrate specificity By similarity HAMAP-Rule MF_01963

Sequences

Sequence LengthMass (Da)Tools
D1YZM1 [UniParc].

Last modified February 9, 2010. Version 1.
Checksum: 1587FDA8FEF0E4B7

FASTA28131,170
        10         20         30         40         50         60 
MVKVGIIGGS GIYDPSMFDH VKEQKVRTPF GTPGDSFIVG SMNGIEAVFL SRHGRGHKYS 

        70         80         90        100        110        120 
PTDLNYRANI YGMKKLGVTH IISVSAVGSL KESLKPLDIV IPDQVYDRTT KRVSTYFEGG 

       130        140        150        160        170        180 
IVAHISFADP FCRKLSDILY ETAKEKYRVH NGGTYLCMEG PQFSTKAESR IYRKLGFDVI 

       190        200        210        220        230        240 
GMTALPEAKL AREAEICFAI LATITDYDVW YEEPVSIGQV IEYAAKNEEA VKDILRRAVG 

       250        260        270        280 
RIEDTDCPCR HALEGAIATS PDAIPEKVKR DLKPLIGPYI K

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References

[1]"Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella paludicola, the first cultivated representative of the order Methanocellales."
Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H., Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R., Mori K., Fujita N., Imachi H., Takai K.
PLoS ONE 6:E22898-E22898(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17711 / JCM 13418 / NBRC 101707 / SANAE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP011532 Genomic DNA. Translation: BAI61893.1.
RefSeqYP_003356876.1. NC_013665.1.

3D structure databases

ProteinModelPortalD1YZM1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAI61893; BAI61893; MCP_1821.
GeneID8681710.
KEGGmpd:MCP_1821.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000228986.
KOK00772.
OMAVVPDQFI.

Enzyme and pathway databases

BioCycMPAL304371:GI7G-1587-MONOMER.
UniPathwayUPA00904; UER00873.

Family and domain databases

HAMAPMF_01963. MTAP.
InterProIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
[Graphical view]
PANTHERPTHR11904. PTHR11904. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01694. MTAP. 1 hit.
ProtoNetSearch...

Entry information

Entry nameD1YZM1_METPS
AccessionPrimary (citable) accession number: D1YZM1
Entry history
Integrated into UniProtKB/TrEMBL: February 9, 2010
Last sequence update: February 9, 2010
Last modified: May 1, 2013
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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