METK2_ACTCC
ID METK2_ACTCC Reviewed; 390 AA.
AC P50302; A0A2R6R7V5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2019, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=S-adenosylmethionine synthase 2;
DE Short=AdoMet synthase 2;
DE EC=2.5.1.6 {ECO:0000250|UniProtKB:Q96551};
DE AltName: Full=Methionine adenosyltransferase 2;
DE Short=MAT 2;
GN Name=SAM2; ORFNames=CEY00_Acc08469 {ECO:0000312|EMBL:PSS23645.1};
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; U17239; AAA81377.1; -; mRNA.
DR EMBL; NKQK01000008; PSS23645.1; -; Genomic_DNA.
DR AlphaFoldDB; P50302; -.
DR SMR; P50302; -.
DR STRING; 1590841.P50302; -.
DR PRIDE; P50302; -.
DR EnsemblPlants; PSS23645; PSS23645; CEY00_Acc08469.
DR Gramene; PSS23645; PSS23645; CEY00_Acc08469.
DR OMA; CERAPDE; -.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000241394; Chromosome lg8.
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 2"
FT /id="PRO_0000174454"
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"
FT CONFLICT 62
FT /note="T -> K (in Ref. 1; AAA81377)"
FT CONFLICT 339
FT /note="K -> E (in Ref. 1; AAA81377)"
FT CONFLICT 378
FT /note="F -> L (in Ref. 1; AAA81377)"
SQ SEQUENCE 390 AA; 42613 MW; 1841E8040F59DD71 CRC64;
MESFLFTSES VNEGHPDKLC DQVSDAILDA CLEQDPESKV ACETCTKTNM VMVFGEITTK
ATVNYEKIVR DTCRGIGFTS PDVGLDADHC KVLVNIEQQS PDIAQGVHGH LSKKPEEIGA
GDQGHMFGYA TDETPELMPL THVLATKLGA KLTEVRKNNT CPWLRPDGKT QVTVEYRNEG
GAMVPVRVHT VLISTQHDET VTNEQIAKDL KEHVIKPVIP AQYMDDDTIF HLNPSGRFVI
GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYVVRQAA KSVVASGLAR
RCIVQVSYAI GVPEPLSVFV DTYKTGKIPD KDILALIKKN FDFRPGMIAI NLDLKRGGNF
RYQKTAAYGH FGRDDADFTW ETVKILKPKA
