METK1_ACTCC
ID METK1_ACTCC Reviewed; 390 AA.
AC P50301; A0A2R6Q9N0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=S-adenosylmethionine synthase 1;
DE Short=AdoMet synthase 1;
DE EC=2.5.1.6 {ECO:0000250|UniProtKB:Q96551};
DE AltName: Full=Methionine adenosyltransferase 1;
DE Short=MAT 1;
GN Name=SAM1; ORFNames=CEY00_Acc20465 {ECO:0000312|EMBL:PSS04609.1};
OS Actinidia chinensis var. chinensis (Chinese soft-hair kiwi).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Actinidiaceae; Actinidia.
OX NCBI_TaxID=1590841;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fruit;
RX PubMed=7630953; DOI=10.1104/pp.108.3.1307;
RA Whittaker D.J., Smith G.S., Gardner R.C.;
RT "Three cDNAs encoding S-adenosyl-L-methionine synthetase from Actinidia
RT chinensis.";
RL Plant Physiol. 108:1307-1308(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Red5;
RX PubMed=29661190; DOI=10.1186/s12864-018-4656-3;
RA Pilkington S.M., Crowhurst R., Hilario E., Nardozza S., Fraser L., Peng Y.,
RA Gunaseelan K., Simpson R., Tahir J., Deroles S.C., Templeton K., Luo Z.,
RA Davy M., Cheng C., McNeilage M., Scaglione D., Liu Y., Zhang Q., Datson P.,
RA De Silva N., Gardiner S.E., Bassett H., Chagne D., McCallum J.,
RA Dzierzon H., Deng C., Wang Y.Y., Barron L., Manako K., Bowen J.,
RA Foster T.M., Erridge Z.A., Tiffin H., Waite C.N., Davies K.M.,
RA Grierson E.P., Laing W.A., Kirk R., Chen X., Wood M., Montefiori M.,
RA Brummell D.A., Schwinn K.E., Catanach A., Fullerton C., Li D.,
RA Meiyalaghan S., Nieuwenhuizen N., Read N., Prakash R., Hunter D., Zhang H.,
RA McKenzie M., Knabel M., Harris A., Allan A.C., Gleave A., Chen A.,
RA Janssen B.J., Plunkett B., Ampomah-Dwamena C., Voogd C., Leif D.,
RA Lafferty D., Souleyre E.J.F., Varkonyi-Gasic E., Gambi F., Hanley J.,
RA Yao J.L., Cheung J., David K.M., Warren B., Marsh K., Snowden K.C.,
RA Lin-Wang K., Brian L., Martinez-Sanchez M., Wang M., Ileperuma N.,
RA Macnee N., Campin R., McAtee P., Drummond R.S.M., Espley R.V.,
RA Ireland H.S., Wu R., Atkinson R.G., Karunairetnam S., Bulley S.,
RA Chunkath S., Hanley Z., Storey R., Thrimawithana A.H., Thomson S.,
RA David C., Testolin R., Huang H., Hellens R.P., Schaffer R.J.;
RT "A manually annotated Actinidia chinensis var. chinensis (kiwifruit) genome
RT highlights the challenges associated with draft genomes and gene prediction
RT in plants.";
RL BMC Genomics 19:257-257(2018).
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:Q96551}.
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:Q96551};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q96551};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q96551};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q96551};
CC Note=Binds 2 divalent ions per subunit. The metal ions interact
CC primarily with the substrate (By similarity). Can utilize magnesium,
CC manganese or cobalt (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:P13444, ECO:0000250|UniProtKB:Q96551};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:Q96551};
CC Note=Binds 1 potassium ion per subunit. The potassium ion interacts
CC primarily with the substrate (By similarity).
CC {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:Q96551}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
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DR EMBL; U17240; AAA81378.1; -; mRNA.
DR EMBL; NKQK01000018; PSS04609.1; -; Genomic_DNA.
DR AlphaFoldDB; P50301; -.
DR SMR; P50301; -.
DR STRING; 1590841.P50301; -.
DR PRIDE; P50301; -.
DR EnsemblPlants; PSS04609; PSS04609; CEY00_Acc20465.
DR Gramene; PSS04609; PSS04609; CEY00_Acc20465.
DR OMA; VACESCT; -.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000241394; Chromosome lg18.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
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 ATP-binding; Cobalt; Cytoplasm; Magnesium; Metal-binding;
KW Nucleotide-binding; One-carbon metabolism; Potassium; Reference proteome;
KW Transferase.
FT CHAIN 1..390
FT /note="S-adenosylmethionine synthase 1"
FT /id="PRO_0000174453"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P13444"
FT BINDING 15
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 43
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 56
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 99
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 390 AA; 42519 MW; E3B66B10112B1E31 CRC64;
MDTFLFTSES VNEGHPDKLC DQVSDAILDA CLKQDPESKV ACESCTKTNM VMVFGEITTK
AQVNYEKIVR DTCRGIGFTS PDVGLDADHC KVLVNIEQQS PDIAQGVHGH LTKKPEEIGA
GDQGHMFGYA TDETPELMPL THVLATKLGA KLTEVRKNST CPWLRPDGKT QVTVEYRNEG
GAMVPIRVHT VLISTQHDET VTNDQIANDL KKHVIKPVVP AQYLDDNTIF HLNPSGRFVI
GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSVVASGLAR
RCLVQVSYAI GVAEPLSVFV DTYKTGKIAD KDILALIKEN FDFRPGMIAI NLDLKRGGNL
RYQKTAAYGH FGRDDPDFTW ETVKILKPKA
