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F6RQL9

- MTAP_MACMU

UniProt

F6RQL9 - MTAP_MACMU

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Protein

S-methyl-5'-thioadenosine phosphorylase

Gene
MTAP
Organism
Macaca mulatta (Rhesus macaque)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei18 – 181Phosphate By similarity
Sitei178 – 1781Important for substrate specificity By similarity
Binding sitei196 – 1961Substrate; via amide nitrogen By similarity
Binding sitei197 – 1971Phosphate By similarity
Sitei233 – 2331Important for substrate specificity By similarity

GO - Molecular functioni

  1. phosphorylase activity Source: InterPro
  2. S-methyl-5-thioadenosine phosphorylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. L-methionine salvage from methylthioadenosine Source: UniProtKB-HAMAP
  2. purine ribonucleoside salvage Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Enzyme and pathway databases

UniPathwayiUPA00904; UER00873.

Names & Taxonomyi

Protein namesi
Recommended name:
S-methyl-5'-thioadenosine phosphorylase (EC:2.4.2.28)
Alternative name(s):
5'-methylthioadenosine phosphorylase
Short name:
MTA phosphorylase
Short name:
MTAP
Short name:
MTAPase
Gene namesi
Name:MTAP
OrganismiMacaca mulatta (Rhesus macaque)
Taxonomic identifieri9544 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca
ProteomesiUP000006718: Chromosome 15

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 283283S-methyl-5'-thioadenosine phosphorylaseUniRule annotationPRO_0000415113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiF6RQL9.

Interactioni

Subunit structurei

Homotrimer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliF6RQL9.
SMRiF6RQL9. Positions 9-281.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni60 – 612Phosphate binding By similarity
Regioni93 – 942Phosphate binding By similarity
Regioni220 – 2223Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

KOiK00772.
OMAiCEAQLCY.
TreeFamiTF312883.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP.
InterProiIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01694. MTAP. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

F6RQL9-1 [UniParc]FASTAAdd to Basket

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MASGTTTTAV KIGIIGGTGL DDPEILEGRT EKYVDTPFGK PSDALILGKI    50
KNVDCVLLAR HGRQHTIMPS KVNYQANIWA LKEEGCTHVI VTTACGSLRE 100
EIQPGDIVII DQFIDRTTMR PQSFYDGSHS CARGVCHIPM AEPFCPKTRE 150
VLIETAKKLG LRCHSKGTMV TIEGPRFSSR AESFMFRTWG ADVINMTTVP 200
EVVLAKEAGI CYASIAMATD YDCWKEHEEA VSVDRVLKTL KENANKAKSL 250
LLTTIPQIGS TEWSETLHNL KNMAQFSVLL PRH 283
Length:283
Mass (Da):31,236
Last modified:July 27, 2011 - v1
Checksum:i3B34C565EB5B99DA
GO

Sequence databases

RefSeqiNP_001248666.1. NM_001261737.1.
UniGeneiMmu.1994.

Genome annotation databases

EnsembliENSMMUT00000001605; ENSMMUP00000001509; ENSMMUG00000001137.
GeneIDi709020.
KEGGimcc:709020.

Cross-referencesi

Sequence databases

RefSeqi NP_001248666.1. NM_001261737.1.
UniGenei Mmu.1994.

3D structure databases

ProteinModelPortali F6RQL9.
SMRi F6RQL9. Positions 9-281.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi F6RQL9.

Proteomic databases

PRIDEi F6RQL9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMMUT00000001605 ; ENSMMUP00000001509 ; ENSMMUG00000001137 .
GeneIDi 709020.
KEGGi mcc:709020.

Organism-specific databases

CTDi 4507.

Phylogenomic databases

KOi K00772.
OMAi CEAQLCY.
TreeFami TF312883.

Enzyme and pathway databases

UniPathwayi UPA00904 ; UER00873 .

Miscellaneous databases

NextBioi 19980238.

Family and domain databases

Gene3Di 3.40.50.1580. 1 hit.
HAMAPi MF_01963. MTAP.
InterProi IPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view ]
PANTHERi PTHR11904. PTHR11904. 1 hit.
Pfami PF01048. PNP_UDP_1. 1 hit.
[Graphical view ]
SUPFAMi SSF53167. SSF53167. 1 hit.
TIGRFAMsi TIGR01694. MTAP. 1 hit.
PROSITEi PS01240. PNP_MTAP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Evolutionary and biomedical insights from the rhesus macaque genome."
    Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C., Makova K.D., Miller W., Milosavljevic A.
    , Palermo R.E., Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., Zwieg A.S.
    Science 316:222-234(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 17573.

Entry informationi

Entry nameiMTAP_MACMU
AccessioniPrimary (citable) accession number: F6RQL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: July 27, 2011
Last modified: June 11, 2014
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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