METK3_CAEEL
ID METK3_CAEEL Reviewed; 404 AA.
AC P50305;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Probable S-adenosylmethionine synthase 3;
DE Short=AdoMet synthase 3;
DE EC=2.5.1.6 {ECO:0000250|UniProtKB:Q00266};
DE AltName: Full=Methionine adenosyltransferase 3;
DE Short=MAT 3;
GN Name=sams-3; ORFNames=C06E7.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP POST-TRANSCRIPTIONAL REGULATION.
RX PubMed=33930289; DOI=10.1016/j.cell.2021.03.062;
RA Mendel M., Delaney K., Pandey R.R., Chen K.M., Wenda J.M., Vaagboe C.B.,
RA Steiner F.A., Homolka D., Pillai R.S.;
RT "Splice site m6A methylation prevents binding of U2AF35 to inhibit RNA
RT splicing.";
RL Cell 0:0-0(2021).
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 -!- INTERACTION:
CC P50305; O17680: sams-1; NbExp=4; IntAct=EBI-2412743, EBI-2412749;
CC -!- MISCELLANEOUS: Protein expression is regulated by post-transcriptional
CC regulation: under rich-diet conditions, mett-10 binds and methylates
CC sams-3 mRNA, directly inhibiting splicing and protein production of S-
CC adenosylmethionine synthase. {ECO:0000269|PubMed:33930289}.
CC -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
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DR EMBL; FO080387; CCD63366.1; -; Genomic_DNA.
DR PIR; T34085; T34085.
DR RefSeq; NP_500872.1; NM_068471.5.
DR AlphaFoldDB; P50305; -.
DR SMR; P50305; -.
DR BioGRID; 42477; 11.
DR IntAct; P50305; 1.
DR STRING; 6239.C06E7.1a; -.
DR EPD; P50305; -.
DR PaxDb; P50305; -.
DR PeptideAtlas; P50305; -.
DR EnsemblMetazoa; C06E7.1a.1; C06E7.1a.1; WBGene00015538.
DR GeneID; 177355; -.
DR KEGG; cel:CELE_C06E7.1; -.
DR UCSC; C06E7.1a; c. elegans.
DR CTD; 177355; -.
DR WormBase; C06E7.1a; CE03957; WBGene00015538; sams-3.
DR eggNOG; KOG1506; Eukaryota.
DR GeneTree; ENSGT00950000183185; -.
DR HOGENOM; CLU_041802_1_1_1; -.
DR InParanoid; P50305; -.
DR OMA; MPYLRPD; -.
DR OrthoDB; 685006at2759; -.
DR PhylomeDB; P50305; -.
DR UniPathway; UPA00315; UER00080.
DR PRO; PR:P50305; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00015538; Expressed in adult organism and 3 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:WormBase.
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; IBA:GO_Central.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW One-carbon metabolism; Potassium; Reference proteome; Transferase.
FT CHAIN 1..404
FT /note="Probable S-adenosylmethionine synthase 3"
FT /id="PRO_0000174442"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P13444"
FT BINDING 17
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 45
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 58
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 101
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 167..169
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 235..238
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 246
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 246
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 252..253
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 269
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 273
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 277
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 277
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"
SQ SEQUENCE 404 AA; 44034 MW; 4F7891933B46E26B CRC64;
MSQHKFLFTS ESVSEGHPDK MCDQISDAVL DAHLAQDPHA KVACETVTKT GMIMLCGEIT
SKAVVDYQVL VRNVIKKIGY DDSSKGFDYK TCNVLVALEQ QSPEIAAGVH VDKDSDDVGA
GDQGIMFGYA TDETEEAMPL TLLLSHKLNR KLHELRRSGE LEWVRPDSKT QVTIEYASEG
GACVPLRVHT VVISTQHSPD ISLDDLRKEL IEKVIKAVIP ANLIDDKTIY HLNPCGSFII
GGPMGDAGLT GRKIIVDTYG GWGAHGGGAF SGKDPTKVDR SAAYAARWVA KSLVKSGLCR
RCLVQVSYAI GVAKPLSVMV FSFGTSALNE GELLKIVNDN FDLRPGMIIK DLDLKKPIYE
PTAENGHFGH NEFPWEQPRH LQIDVELLKK IGGKTISNGN GIAH
