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Q8CXR2 (MTAP_LEPIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:LA_4248
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) [Reference proteome] [HAMAP]
Taxonomic identifier189518 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length287 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 – 287287S-methyl-5'-thioadenosine phosphorylase HAMAP-Rule MF_01963
PRO_0000184550

Regions

Region55 – 562Phosphate 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
Site2231Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8CXR2 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 2830C5FB62F3AE88

FASTA28732,031
        10         20         30         40         50         60 
MSYNVRAAII GGTGLYSLEG MELIEEIFPD TPWGKPSDKI KIGKYKGKLI AFLPRHGIGH 

        70         80         90        100        110        120 
FLSPPEVPNH ANICALKQLG VEEIVAFSSV GSLREEIKPL DFVLPSQIID RTRFRNSTYF 

       130        140        150        160        170        180 
GNGVVAHAPF AEPFSPNLSK RIAQTAKKIG LEIHLDKTLV CMEGPLFSTK AESHLYRSWG 

       190        200        210        220        230        240 
ADIINMTVLP EAKLAREAEI AYQMICMSTD YDCWREGEES VTVEMVIANL TKNAETAKKL 

       250        260        270        280 
LSELIHVLGN GDDLSLKNST RYSIITAPEK RNSETVKKLR VLFPEYF 

« Hide

References

[1]"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing."
Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H. expand/collapse author list , Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.
Nature 422:888-893(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 56601.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010300 Genomic DNA. Translation: AAN51446.1.
RefSeqNP_714428.1. NC_004342.2.

3D structure databases

ProteinModelPortalQ8CXR2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING189518.LA4248.

Proteomic databases

PaxDbQ8CXR2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN51446; AAN51446; LA_4248.
GeneID1153590.
KEGGlil:LA_4248.
PATRIC22389337. VBILepInt91350_4221.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228986.
KOK00772.
OMACEAQLCY.
OrthoDBEOG6KHFXC.

Enzyme and pathway databases

BioCycLINT189518:GJBB-3366-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_LEPIN
AccessionPrimary (citable) accession number: Q8CXR2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 67 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