METK1_BOVIN
ID METK1_BOVIN Reviewed; 396 AA.
AC Q2KJC6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=S-adenosylmethionine synthase isoform type-1;
DE Short=AdoMet synthase 1;
DE EC=2.5.1.6 {ECO:0000250|UniProtKB:P13444};
DE AltName: Full=Methionine adenosyltransferase 1;
DE Short=MAT 1;
GN Name=MAT1A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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:P13444}.
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:P13444};
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:P13444}.
CC -!- SUBUNIT: Homotetramer (MAT-I); dimer of dimers. Homodimer (MAT-III).
CC {ECO:0000250|UniProtKB:P13444}.
CC -!- PTM: S-nitrosylation of Cys-121 inactivates the enzyme.
CC {ECO:0000250|UniProtKB:P13444}.
CC -!- PTM: An intrachain disulfide bond can be formed. The protein structure
CC shows that the relevant Cys residues are in a position that would
CC permit formation of a disulfide bond. {ECO:0000250|UniProtKB:P13444}.
CC -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
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DR EMBL; BC105410; AAI05411.1; -; mRNA.
DR RefSeq; NP_001039962.1; NM_001046497.1.
DR AlphaFoldDB; Q2KJC6; -.
DR SMR; Q2KJC6; -.
DR STRING; 9913.ENSBTAP00000031255; -.
DR PaxDb; Q2KJC6; -.
DR PeptideAtlas; Q2KJC6; -.
DR PRIDE; Q2KJC6; -.
DR GeneID; 541078; -.
DR KEGG; bta:541078; -.
DR CTD; 4143; -.
DR eggNOG; KOG1506; Eukaryota.
DR InParanoid; Q2KJC6; -.
DR OrthoDB; 685006at2759; -.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000009136; Unplaced.
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:UniProtKB.
DR GO; GO:0009087; P:methionine catabolic process; ISS:UniProtKB.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; ISS:UniProtKB.
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; Disulfide bond; Magnesium; Metal-binding; Nucleotide-binding;
KW One-carbon metabolism; Potassium; Reference proteome; S-nitrosylation;
KW Transferase.
FT CHAIN 1..396
FT /note="S-adenosylmethionine synthase isoform type-1"
FT /id="PRO_0000287527"
FT REGION 114..126
FT /note="Flexible loop"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 24
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P13444"
FT BINDING 30
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:P13444"
FT BINDING 58
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 71
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 114
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 180..182
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 248..251
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 259
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:P13444"
FT BINDING 259
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 265..266
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 282
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 286
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 290
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 290
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 MOD_RES 121
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P13444"
FT DISULFID 35..61
FT /evidence="ECO:0000250|UniProtKB:P13444"
SQ SEQUENCE 396 AA; 43761 MW; 2188750981D65CDB CRC64;
MNGPVDGLCD HSLSEEGAFM FTSESVGEGH PDKICDQISD AVLDAHLKQD PNAKVACETV
CKTGMVLLCG EITSMAMVDY QRVVRETIQH IGYDDSAKGF DFKTCNVLVA LEQQSPDIAQ
CVHLDRNEED VGAGDQGLMF GYATDETEEC MPLTIMLAHR LNARMAELRR SGQLPWLQPD
SKTQVTVQYT QDNGAVIPMR VHTVVISVQH NEDITLEDMR RALKEQVIRA VVPARYLDED
TIYHLQPSGR FVIGGPQGDA GVTGRKIIVD TYGGWGAHGG GAFSGKDYTK VDRSAAYAAR
WVAKSLVKAG LCRRVLVQVS YAIGVAEPLS ISIFTYGTSQ KTERELLDVV NKNFDLRPGV
IVRDLDLKKP IYQKTACYGH FGRSEFPWEV PKKLVF
