MTAP_DROME
ID MTAP_DROME Reviewed; 289 AA.
AC Q9V813;
DT 24-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=S-methyl-5'-thioadenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_03155};
DE EC=2.4.2.28 {ECO:0000255|HAMAP-Rule:MF_03155};
DE AltName: Full=5'-methylthioadenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_03155};
DE Short=MTA phosphorylase {ECO:0000255|HAMAP-Rule:MF_03155};
DE Short=MTAP {ECO:0000255|HAMAP-Rule:MF_03155};
DE Short=MTAPase {ECO:0000255|HAMAP-Rule:MF_03155};
GN Name=Mtap; ORFNames=CG4802;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Ovary;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17534888; DOI=10.1002/ajmg.a.31724;
RA Williamson R.E., Darrow K.N., Michaud S., Jacobs J.S., Jones M.C.,
RA Eberl D.F., Maas R.L., Liberman M.C., Morton C.C.;
RT "Methylthioadenosine phosphorylase (MTAP) in hearing: gene disruption by
RT chromosomal rearrangement in a hearing impaired individual and model
RT organism analysis.";
RL Am. J. Med. Genet. A 143:1630-1639(2007).
CC -!- FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'-
CC thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate.
CC Involved in the breakdown of MTA, a major by-product of polyamine
CC biosynthesis. Responsible for the first step in the methionine salvage
CC pathway after MTA has been generated from S-adenosylmethionine. Has
CC broad substrate specificity with 6-aminopurine nucleosides as preferred
CC substrates. {ECO:0000255|HAMAP-Rule:MF_03155}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5-
CC thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:11852,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58533; EC=2.4.2.28; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03155};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-
CC thioadenosine (phosphorylase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_03155}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_03155}.
CC -!- INTERACTION:
CC Q9V813; Q9V813: Mtap; NbExp=4; IntAct=EBI-124076, EBI-124076;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03155}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03155}.
CC -!- TISSUE SPECIFICITY: In embryos, expressed in the fat body and visceral
CC mesoderm. {ECO:0000269|PubMed:17534888}.
CC -!- DISRUPTION PHENOTYPE: No visible auditory phenotype.
CC {ECO:0000269|PubMed:17534888}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03155}.
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DR EMBL; AE013599; AAF57869.1; -; Genomic_DNA.
DR EMBL; BT004912; AAO49165.1; -; mRNA.
DR RefSeq; NP_001286525.1; NM_001299596.1.
DR RefSeq; NP_611208.1; NM_137364.4.
DR AlphaFoldDB; Q9V813; -.
DR SMR; Q9V813; -.
DR BioGRID; 62649; 5.
DR DIP; DIP-20687N; -.
DR IntAct; Q9V813; 15.
DR STRING; 7227.FBpp0086072; -.
DR PaxDb; Q9V813; -.
DR PRIDE; Q9V813; -.
DR DNASU; 36955; -.
DR EnsemblMetazoa; FBtr0086916; FBpp0086072; FBgn0034215.
DR EnsemblMetazoa; FBtr0345803; FBpp0311789; FBgn0034215.
DR GeneID; 36955; -.
DR KEGG; dme:Dmel_CG4802; -.
DR UCSC; CG4802-RA; d. melanogaster.
DR CTD; 4507; -.
DR FlyBase; FBgn0034215; Mtap.
DR VEuPathDB; VectorBase:FBgn0034215; -.
DR eggNOG; KOG3985; Eukaryota.
DR GeneTree; ENSGT00950000182991; -.
DR HOGENOM; CLU_054456_0_0_1; -.
DR InParanoid; Q9V813; -.
DR OMA; ADPFCPE; -.
DR OrthoDB; 1616485at2759; -.
DR PhylomeDB; Q9V813; -.
DR Reactome; R-DME-1237112; Methionine salvage pathway.
DR UniPathway; UPA00904; UER00873.
DR BioGRID-ORCS; 36955; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36955; -.
DR PRO; PR:Q9V813; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034215; Expressed in capitellum (Drosophila) and 27 other tissues.
DR ExpressionAtlas; Q9V813; baseline and differential.
DR Genevisible; Q9V813; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IBA:GO_Central.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR CDD; cd09010; MTAP_SsMTAPII_like_MTIP; 1.
DR Gene3D; 3.40.50.1580; -; 1.
DR HAMAP; MF_01963; MTAP; 1.
DR InterPro; IPR010044; MTAP.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR018099; Purine_phosphorylase-2_CS.
DR PANTHER; PTHR42679; PTHR42679; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR01694; MTAP; 1.
DR PROSITE; PS01240; PNP_MTAP_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycosyltransferase; Nucleus; Purine salvage;
KW Reference proteome; Transferase.
FT CHAIN 1..289
FT /note="S-methyl-5'-thioadenosine phosphorylase"
FT /id="PRO_0000184548"
FT BINDING 24
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT BINDING 66..67
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT BINDING 99..100
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT BINDING 203
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT BINDING 226..228
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT SITE 184
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT SITE 239
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
SQ SEQUENCE 289 AA; 32018 MW; 387328BCAFD5E6D9 CRC64;
MITIKCKDTN LDPLPVKIGI IGGSGLDDPD ILEQRQERVV ETPYGEPSDA LIEGEINGVQ
CVLLARHGRK HDIMPSNVNY RANIWALRDV GCTHLIVSTA CGSLREEIKP GNLVVPHDFI
DRTTKRLQTF YDGKAQSPRG VCHLPMFPAF SERTRNILLQ AAKELEIPAH DKATIVTIEG
PRFSSRSESH MFRQWGGDLI NMTTCPEVVL AKEAGLLYGS VAIATDYDCW RMGCEGVNVQ
DVLRTFAENV IKVKKILVNA VGRIAKEDWS EDILNAKQCV CNNTMSGAM
