METK1_BRAJU
ID METK1_BRAJU Reviewed; 393 AA.
AC P49611;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=SAMS1;
OS Brassica juncea (Indian mustard) (Sinapis juncea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3707;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. India mustard; TISSUE=Leaf;
RX PubMed=7716233; DOI=10.1104/pp.107.3.1021;
RA Wen C.-M., Wu M., Goh C.-J., Pua E.-C.;
RT "Cloning and nucleotide sequence of a cDNA encoding S-adenosyl-L-methionine
RT synthetase from mustard (Brassica juncea [L.] Czern & Coss).";
RL Plant Physiol. 107:1021-1022(1995).
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; X80362; CAA56590.1; -; mRNA.
DR AlphaFoldDB; P49611; -.
DR SMR; P49611; -.
DR PRIDE; P49611; -.
DR UniPathway; UPA00315; UER00080.
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; Transferase.
FT CHAIN 1..393
FT /note="S-adenosylmethionine synthase 1"
FT /id="PRO_0000174458"
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 393 AA; 43226 MW; 50188D87C5EE41FA CRC64;
METFLFTSES VNEGHPDKLC DQISDAVLDA CLEQDPDSKV ACETCTKTNM VMVFGEITTK
ATVDYEKIVR DTCRSIGFIS DDVGLDADKC KVLVNIEQQS PDIAQGVHGH FTKRPEDIGA
GDQGHMFGYA TDETPELMPL SHVLATKIGA KLTEVRKNGT CRWLRPDGKT QVTVEYYNDN
GAMVPVRVHT VLISTQHDET VTNEEIARDL KEHVIKPIIP EKYLDDKTIF HLNPSGRFVI
GGPDGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQSA KSVVANGMAR
RALVQVSYAI GVPEPFSVFV DTYGTGLIPD KEILKIVKES FDFRPGMMTI NLDLKRGGNG
RFLKTAAYGH FGRDDPDFTW EVVKPLKWDK PQA
