METK_DROME
ID METK_DROME Reviewed; 408 AA.
AC P40320; Q0E8V3; Q9VPJ2; Q9VPJ3; Q9VPJ4; Q9VPJ5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=S-adenosylmethionine synthase;
DE Short=AdoMet synthase;
DE EC=2.5.1.6 {ECO:0000250|UniProtKB:Q00266};
DE AltName: Full=Methionine adenosyltransferase;
DE Short=MAT;
GN Name=Sam-S; Synonyms=M(2)21AB, SamS; ORFNames=CG2674;
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 [MRNA] (ISOFORM 2), AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S; TISSUE=Pupae;
RX PubMed=8150093; DOI=10.1016/0014-5793(94)80526-1;
RA Larsson J., Rasmuson-Lestander A.;
RT "Molecular cloning of the S-adenosylmethionine synthetase gene in
RT Drosophila melanogaster.";
RL FEBS Lett. 342:329-333(1994).
RN [2]
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 [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC methionine and ATP. The reaction comprises two steps that are both
CC catalyzed by the same enzyme: formation of S-adenosylmethionine
CC (AdoMet) and triphosphate, and subsequent hydrolysis of the
CC triphosphate. {ECO:0000250|UniProtKB:Q00266}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-
CC adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6;
CC Evidence={ECO:0000250|UniProtKB:Q00266};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P13444};
CC Note=Binds 2 magnesium ions per subunit. The magnesium ions interact
CC primarily with the substrate. {ECO:0000250|UniProtKB:P13444};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:P13444};
CC Note=Binds 1 potassium ion per subunit. The potassium ion interacts
CC primarily with the substrate. {ECO:0000250|UniProtKB:P13444};
CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC S-adenosyl-L-methionine from L-methionine: step 1/1.
CC {ECO:0000250|UniProtKB:Q00266}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=2; Synonyms=A, D;
CC IsoId=P40320-1; Sequence=Displayed;
CC Name=1; Synonyms=B;
CC IsoId=P40320-2; Sequence=VSP_005963, VSP_005964, VSP_005965;
CC Name=3; Synonyms=C, J;
CC IsoId=P40320-3; Sequence=VSP_005963;
CC Name=4; Synonyms=G;
CC IsoId=P40320-4; Sequence=VSP_005961, VSP_005962, VSP_005963;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed throughout development with highest levels at adult stages.
CC {ECO:0000269|PubMed:8150093}.
CC -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
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DR EMBL; X77392; CAA54567.1; -; mRNA.
DR EMBL; AE014134; AAF51555.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF51556.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF51557.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF51558.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10505.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10506.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10507.1; -; Genomic_DNA.
DR EMBL; AE014134; AAS64636.1; -; Genomic_DNA.
DR EMBL; AY051918; AAK93342.1; -; mRNA.
DR PIR; S43258; S41917.
DR RefSeq; NP_524923.1; NM_080184.2. [P40320-3]
DR RefSeq; NP_722593.1; NM_164355.3. [P40320-3]
DR RefSeq; NP_722594.1; NM_164356.2. [P40320-1]
DR RefSeq; NP_722595.1; NM_164357.2. [P40320-1]
DR RefSeq; NP_722596.1; NM_164358.2. [P40320-1]
DR RefSeq; NP_722597.1; NM_164359.2. [P40320-1]
DR RefSeq; NP_722598.1; NM_164360.3. [P40320-1]
DR RefSeq; NP_722599.1; NM_164361.2. [P40320-2]
DR RefSeq; NP_722600.1; NM_164362.3. [P40320-4]
DR RefSeq; NP_995602.1; NM_205880.1. [P40320-1]
DR AlphaFoldDB; P40320; -.
DR SMR; P40320; -.
DR BioGRID; 71491; 26.
DR DIP; DIP-18340N; -.
DR IntAct; P40320; 9.
DR STRING; 7227.FBpp0088926; -.
DR PaxDb; P40320; -.
DR PRIDE; P40320; -.
DR DNASU; 48552; -.
DR EnsemblMetazoa; FBtr0089428; FBpp0088444; FBgn0005278. [P40320-2]
DR EnsemblMetazoa; FBtr0089429; FBpp0088445; FBgn0005278. [P40320-1]
DR EnsemblMetazoa; FBtr0089430; FBpp0088446; FBgn0005278. [P40320-1]
DR EnsemblMetazoa; FBtr0089431; FBpp0088447; FBgn0005278. [P40320-3]
DR EnsemblMetazoa; FBtr0089432; FBpp0088448; FBgn0005278. [P40320-1]
DR EnsemblMetazoa; FBtr0089433; FBpp0088449; FBgn0005278. [P40320-1]
DR EnsemblMetazoa; FBtr0089434; FBpp0088450; FBgn0005278. [P40320-1]
DR EnsemblMetazoa; FBtr0089435; FBpp0088451; FBgn0005278. [P40320-3]
DR EnsemblMetazoa; FBtr0089436; FBpp0088452; FBgn0005278. [P40320-4]
DR EnsemblMetazoa; FBtr0089437; FBpp0088926; FBgn0005278. [P40320-1]
DR GeneID; 48552; -.
DR KEGG; dme:Dmel_CG2674; -.
DR CTD; 48552; -.
DR FlyBase; FBgn0005278; Sam-S.
DR VEuPathDB; VectorBase:FBgn0005278; -.
DR eggNOG; KOG1506; Eukaryota.
DR GeneTree; ENSGT00950000183185; -.
DR HOGENOM; CLU_041802_0_1_1; -.
DR InParanoid; P40320; -.
DR OMA; MPYLRPD; -.
DR PhylomeDB; P40320; -.
DR SignaLink; P40320; -.
DR UniPathway; UPA00315; UER00080.
DR BioGRID-ORCS; 48552; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Sam-S; fly.
DR GenomeRNAi; 48552; -.
DR PRO; PR:P40320; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0005278; Expressed in capitellum (Drosophila) and 43 other tissues.
DR ExpressionAtlas; P40320; baseline and differential.
DR Genevisible; P40320; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004478; F:methionine adenosyltransferase activity; ISS:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IMP:FlyBase.
DR HAMAP; MF_00086; S_AdoMet_synth1; 1.
DR InterPro; IPR022631; ADOMET_SYNTHASE_CS.
DR InterPro; IPR022630; S-AdoMet_synt_C.
DR InterPro; IPR022629; S-AdoMet_synt_central.
DR InterPro; IPR022628; S-AdoMet_synt_N.
DR InterPro; IPR002133; S-AdoMet_synthetase.
DR InterPro; IPR022636; S-AdoMet_synthetase_sfam.
DR PANTHER; PTHR11964; PTHR11964; 1.
DR Pfam; PF02773; S-AdoMet_synt_C; 1.
DR Pfam; PF02772; S-AdoMet_synt_M; 1.
DR Pfam; PF00438; S-AdoMet_synt_N; 1.
DR PIRSF; PIRSF000497; MAT; 1.
DR SUPFAM; SSF55973; SSF55973; 3.
DR TIGRFAMs; TIGR01034; metK; 1.
DR PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
DR PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Magnesium; Metal-binding;
KW Nucleotide-binding; One-carbon metabolism; Potassium; Reference proteome;
KW Transferase.
FT CHAIN 1..408
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_0000174446"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P13444"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q00266"
FT BINDING 68
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 81
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 124
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 190..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q00266"
FT BINDING 258..261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q00266"
FT BINDING 269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q00266"
FT BINDING 269
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 275..276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P13444"
FT BINDING 300
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT VAR_SEQ 1..27
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_005961"
FT VAR_SEQ 28..41
FT /note="TFLFTSESVGEGHP -> MISAECHSEEYTPN (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_005962"
FT VAR_SEQ 112..141
FT /note="FKTCNVLLALDQQSPEIAAGVHVNRAEEEI -> WKTLNLLVAIEQQSPNIA
FT NGVHINREEEDV (in isoform 1, isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_005963"
FT VAR_SEQ 147..200
FT /note="GIMFGYATDETEECMPLTVVLAHKLNEKIAELRRSDVFWWARPDSKTQVTCE
FT YL -> VSISKRAMCCWHWTNNRLRSLRECMSTVPRKRSVPEIRVSCLDMPPTKPRNVC
FT P (in isoform 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_005964"
FT VAR_SEQ 201..408
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_005965"
FT CONFLICT 34
FT /note="E -> V (in Ref. 1; CAA54567)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="V -> I (in Ref. 1; CAA54567)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="G -> A (in Ref. 1; CAA54567)"
FT /evidence="ECO:0000305"
FT CONFLICT 400..408
FT /note="EAKPLEIDN -> SQASGD (in Ref. 1; CAA54567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 44697 MW; CA0F97C1EA6623DF CRC64;
MPQKTNGHSA NGCNGSNGNS YDMEDGATFL FTSESVGEGH PDKMCDQISD AILDAHLKQD
PNAKVACETV AKTGMILLCG EITSKAVVDY QKVVRETVQH IGYDDSSKGF DFKTCNVLLA
LDQQSPEIAA GVHVNRAEEE IGAGDQGIMF GYATDETEEC MPLTVVLAHK LNEKIAELRR
SDVFWWARPD SKTQVTCEYL FNQGSAVPKR VHTIVVSMQH SEKISLETLR SEVMEKVVKV
VIPAKYIDAN TIVHINPCGL FVIGGPMGDA GLTGRKIIVD TYGGWGAHGG GAFSGKDFTK
VDRSAAYAAR WVAKSLVKAG LCKRCLVQVS YAIGLAEPLS ITVFDYGTSH KSQKELLDII
RRNFDLRPGK IVKDLNLRQP IYQRTSTYGH FGRAGFSWEE AKPLEIDN
