METK_PYRFU
ID METK_PYRFU Reviewed; 401 AA.
AC Q8TZW1;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=S-adenosylmethionine synthase {ECO:0000255|HAMAP-Rule:MF_00136};
DE Short=AdoMet synthase {ECO:0000255|HAMAP-Rule:MF_00136};
DE EC=2.5.1.6 {ECO:0000255|HAMAP-Rule:MF_00136};
DE AltName: Full=Methionine adenosyltransferase {ECO:0000255|HAMAP-Rule:MF_00136};
GN Name=mat {ECO:0000255|HAMAP-Rule:MF_00136}; OrderedLocusNames=PF1866;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC methionine and ATP. {ECO:0000255|HAMAP-Rule:MF_00136}.
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:0000255|HAMAP-Rule:MF_00136};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00136};
CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC S-adenosyl-L-methionine from L-methionine: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00136}.
CC -!- SIMILARITY: Belongs to the AdoMet synthase 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00136}.
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DR EMBL; AE009950; AAL81990.1; -; Genomic_DNA.
DR RefSeq; WP_011013005.1; NZ_CP023154.1.
DR PDB; 6S81; X-ray; 1.78 A; A/B/C/D=1-401.
DR PDB; 6S83; X-ray; 2.34 A; A/B/C/D/E/F/G/H=1-401.
DR PDBsum; 6S81; -.
DR PDBsum; 6S83; -.
DR AlphaFoldDB; Q8TZW1; -.
DR SMR; Q8TZW1; -.
DR STRING; 186497.PF1866; -.
DR EnsemblBacteria; AAL81990; AAL81990; PF1866.
DR GeneID; 41713686; -.
DR KEGG; pfu:PF1866; -.
DR PATRIC; fig|186497.12.peg.1936; -.
DR eggNOG; arCOG01678; Archaea.
DR HOGENOM; CLU_057642_0_0_2; -.
DR OMA; IGHPDSI; -.
DR OrthoDB; 21658at2157; -.
DR PhylomeDB; Q8TZW1; -.
DR BRENDA; 2.5.1.6; 5243.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.300.280; -; 2.
DR HAMAP; MF_00136; S_AdoMet_synth2; 1.
DR InterPro; IPR027790; AdoMet_synthase_2_family.
DR InterPro; IPR042544; AdoMet_synthase_3.
DR InterPro; IPR002795; S-AdoMet_synthetase_arc.
DR PANTHER; PTHR36697; PTHR36697; 1.
DR Pfam; PF01941; AdoMet_Synthase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Magnesium; Nucleotide-binding;
KW One-carbon metabolism; Reference proteome; Transferase.
FT CHAIN 1..401
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_0000150037"
FT BINDING 136..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00136"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:6S81"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:6S81"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:6S81"
FT HELIX 31..54
FT /evidence="ECO:0007829|PDB:6S81"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:6S81"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6S81"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:6S81"
FT STRAND 85..97
FT /evidence="ECO:0007829|PDB:6S81"
FT HELIX 104..119
FT /evidence="ECO:0007829|PDB:6S81"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:6S81"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:6S81"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:6S81"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:6S81"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:6S83"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:6S81"
FT HELIX 171..183
FT /evidence="ECO:0007829|PDB:6S81"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:6S81"
FT STRAND 195..206
FT /evidence="ECO:0007829|PDB:6S81"
FT STRAND 209..219
FT /evidence="ECO:0007829|PDB:6S81"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:6S81"
FT HELIX 226..247
FT /evidence="ECO:0007829|PDB:6S81"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:6S81"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:6S81"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:6S81"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:6S81"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:6S81"
FT HELIX 314..332
FT /evidence="ECO:0007829|PDB:6S81"
FT STRAND 335..343
FT /evidence="ECO:0007829|PDB:6S81"
FT STRAND 354..362
FT /evidence="ECO:0007829|PDB:6S81"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:6S81"
FT HELIX 372..384
FT /evidence="ECO:0007829|PDB:6S81"
FT HELIX 386..394
FT /evidence="ECO:0007829|PDB:6S81"
SQ SEQUENCE 401 AA; 44281 MW; 4E764C50A5F25B8C CRC64;
MARNIVVEEI VRTPVEMQQV ELVERKGIGH PDSIADGIAE AVSRALCREY IRRYGVILHH
NTDQVEVVGG RAYPRFGGGE VVKPIYILLS GRAVELVDQE LFPVHEVAIK AAKNYLKNAI
RHLDVENHVI IDSRIGQGSV DLVSVFNKAR ENPIPLANDT SFGVGYAPLS ETERLVLETE
KLLNSEKFKK EYPAVGEDIK VMGLRRGNEI DLTIAAAIVD SEVATPKEYL EVKDKIKEAV
EELAKEITSR KVNIYVNTAD DPERGIYYIT VTGTSAEAGD DGSVGRGNRV NGLITPNRHM
SMEAAAGKNP VSHVGKIYNI LAMLIAEDIA KTLPVEEVYV RILSQIGKPI DQPLVASIQV
IPKPGHSVKE FEKDAYSIAD EWLANITKVQ KMILEDKISV F
