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Protein

S-methyl-5'-thioadenosine phosphorylase

Gene

Mtap

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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.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 sitei24 – 241PhosphateUniRule annotation
Sitei184 – 1841Important for substrate specificityUniRule annotation
Binding sitei202 – 2021Substrate; via amide nitrogenUniRule annotation
Binding sitei203 – 2031PhosphateUniRule annotation
Sitei239 – 2391Important for substrate specificityUniRule annotation

GO - Molecular functioni

  1. phosphorylase activity Source: InterPro
  2. purine-nucleoside phosphorylase activity Source: GO_Central
  3. S-methyl-5-thioadenosine phosphorylase activity Source: GO_Central

GO - Biological processi

  1. L-methionine biosynthetic process from methylthioadenosine Source: UniProtKB-HAMAP
  2. purine-containing compound salvage Source: GO_Central
  3. purine ribonucleoside salvage Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Enzyme and pathway databases

ReactomeiREACT_335690. Methionine salvage pathway.
SignaLinkiQ9V813.
UniPathwayiUPA00904; UER00873.

Names & Taxonomyi

Protein namesi
Recommended name:
S-methyl-5'-thioadenosine phosphorylaseUniRule annotation (EC:2.4.2.28UniRule annotation)
Alternative name(s):
5'-methylthioadenosine phosphorylaseUniRule annotation
Short name:
MTA phosphorylaseUniRule annotation
Short name:
MTAPUniRule annotation
Short name:
MTAPaseUniRule annotation
Gene namesi
Name:Mtap
ORF Names:CG4802
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0034215. Mtap.

Subcellular locationi

  1. Cytoplasm UniRule annotation
  2. Nucleus UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible auditory phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 289289S-methyl-5'-thioadenosine phosphorylasePRO_0000184548Add
BLAST

Proteomic databases

PaxDbiQ9V813.
PRIDEiQ9V813.

Expressioni

Tissue specificityi

In embryos, expressed in the fat body and visceral mesoderm.1 Publication

Gene expression databases

BgeeiQ9V813.

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

BioGridi62649. 5 interactions.
DIPiDIP-20687N.
IntActiQ9V813. 15 interactions.
MINTiMINT-287272.
STRINGi7227.FBpp0086072.

Structurei

3D structure databases

ProteinModelPortaliQ9V813.
SMRiQ9V813. Positions 16-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni66 – 672Phosphate bindingUniRule annotation
Regioni99 – 1002Phosphate bindingUniRule annotation
Regioni226 – 2283Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0005.
GeneTreeiENSGT00550000074874.
InParanoidiQ9V813.
KOiK00772.
OrthoDBiEOG771270.
PhylomeDBiQ9V813.

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.

Q9V813-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITIKCKDTN LDPLPVKIGI IGGSGLDDPD ILEQRQERVV ETPYGEPSDA
60 70 80 90 100
LIEGEINGVQ CVLLARHGRK HDIMPSNVNY RANIWALRDV GCTHLIVSTA
110 120 130 140 150
CGSLREEIKP GNLVVPHDFI DRTTKRLQTF YDGKAQSPRG VCHLPMFPAF
160 170 180 190 200
SERTRNILLQ AAKELEIPAH DKATIVTIEG PRFSSRSESH MFRQWGGDLI
210 220 230 240 250
NMTTCPEVVL AKEAGLLYGS VAIATDYDCW RMGCEGVNVQ DVLRTFAENV
260 270 280
IKVKKILVNA VGRIAKEDWS EDILNAKQCV CNNTMSGAM
Length:289
Mass (Da):32,018
Last modified:May 1, 2000 - v1
Checksum:i387328BCAFD5E6D9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF57869.1.
BT004912 mRNA. Translation: AAO49165.1.
RefSeqiNP_001286525.1. NM_001299596.1.
NP_611208.1. NM_137364.4.
UniGeneiDm.11469.

Genome annotation databases

EnsemblMetazoaiFBtr0086916; FBpp0086072; FBgn0034215.
FBtr0345803; FBpp0311789; FBgn0034215.
GeneIDi36955.
KEGGidme:Dmel_CG4802.
UCSCiCG4802-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF57869.1.
BT004912 mRNA. Translation: AAO49165.1.
RefSeqiNP_001286525.1. NM_001299596.1.
NP_611208.1. NM_137364.4.
UniGeneiDm.11469.

3D structure databases

ProteinModelPortaliQ9V813.
SMRiQ9V813. Positions 16-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62649. 5 interactions.
DIPiDIP-20687N.
IntActiQ9V813. 15 interactions.
MINTiMINT-287272.
STRINGi7227.FBpp0086072.

Proteomic databases

PaxDbiQ9V813.
PRIDEiQ9V813.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086916; FBpp0086072; FBgn0034215.
FBtr0345803; FBpp0311789; FBgn0034215.
GeneIDi36955.
KEGGidme:Dmel_CG4802.
UCSCiCG4802-RA. d. melanogaster.

Organism-specific databases

CTDi4507.
FlyBaseiFBgn0034215. Mtap.

Phylogenomic databases

eggNOGiCOG0005.
GeneTreeiENSGT00550000074874.
InParanoidiQ9V813.
KOiK00772.
OrthoDBiEOG771270.
PhylomeDBiQ9V813.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00873.
ReactomeiREACT_335690. Methionine salvage pathway.
SignaLinkiQ9V813.

Miscellaneous databases

GenomeRNAii36955.
NextBioi801212.
PROiQ9V813.

Gene expression databases

BgeeiQ9V813.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Ovary.
  4. "Methylthioadenosine phosphorylase (MTAP) in hearing: gene disruption by chromosomal rearrangement in a hearing impaired individual and model organism analysis."
    Williamson R.E., Darrow K.N., Michaud S., Jacobs J.S., Jones M.C., Eberl D.F., Maas R.L., Liberman M.C., Morton C.C.
    Am. J. Med. Genet. A 143:1630-1639(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiMTAP_DROME
AccessioniPrimary (citable) accession number: Q9V813
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 24, 2002
Last sequence update: May 1, 2000
Last modified: April 29, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.