METK_SACS2
ID METK_SACS2 Reviewed; 404 AA.
AC Q980S9;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 100.
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=SSO0199;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK40544.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006641; AAK40544.1; ALT_INIT; Genomic_DNA.
DR PIR; A90161; A90161.
DR RefSeq; WP_009990439.1; NC_002754.1.
DR PDB; 4HPV; X-ray; 2.21 A; A/B=1-404.
DR PDB; 4K0B; X-ray; 2.39 A; A/B=1-404.
DR PDB; 4L2Z; X-ray; 2.49 A; A/B=1-404.
DR PDB; 4L7I; X-ray; 2.19 A; A/B=1-404.
DR PDB; 4WS9; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-404.
DR PDBsum; 4HPV; -.
DR PDBsum; 4K0B; -.
DR PDBsum; 4L2Z; -.
DR PDBsum; 4L7I; -.
DR PDBsum; 4WS9; -.
DR AlphaFoldDB; Q980S9; -.
DR SMR; Q980S9; -.
DR MINT; Q980S9; -.
DR STRING; 273057.SSO0199; -.
DR EnsemblBacteria; AAK40544; AAK40544; SSO0199.
DR GeneID; 27426493; -.
DR KEGG; sso:SSO0199; -.
DR PATRIC; fig|273057.12.peg.198; -.
DR eggNOG; arCOG01678; Archaea.
DR HOGENOM; CLU_057642_0_0_2; -.
DR InParanoid; Q980S9; -.
DR OMA; IGHPDSI; -.
DR PhylomeDB; Q980S9; -.
DR BRENDA; 2.5.1.6; 6163.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000001974; 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..404
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_0000150041"
FT BINDING 139..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00136"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:4L7I"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:4HPV"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:4L7I"
FT HELIX 30..53
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:4L7I"
FT HELIX 107..122
FT /evidence="ECO:0007829|PDB:4L7I"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:4L7I"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:4L7I"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:4L7I"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 196..207
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 210..220
FT /evidence="ECO:0007829|PDB:4L7I"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:4L7I"
FT HELIX 227..248
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:4L7I"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:4L7I"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:4L7I"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:4L7I"
FT HELIX 316..334
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 338..346
FT /evidence="ECO:0007829|PDB:4L7I"
FT STRAND 357..368
FT /evidence="ECO:0007829|PDB:4L7I"
FT HELIX 372..386
FT /evidence="ECO:0007829|PDB:4L7I"
FT HELIX 389..397
FT /evidence="ECO:0007829|PDB:4L7I"
SQ SEQUENCE 404 AA; 44663 MW; F6BD144BC36861C4 CRC64;
MRNINVQLNP LSDIEKLQVE LVERKGLGHP DYIADAVAEE ASRKLSLYYL KKYGVILHHN
LDKTLVVGGQ ATPRFKGGDI IQPIYIIVAG RATTEVKTES GIDQIPVGTI IIESVKEWIR
NNFRYLDAER HVIVDYKIGK GSSDLVGIFE ASKRVPLSND TSFGVGFAPL TKLEKLVYET
ERHLNSKQFK AKLPEVGEDI KVMGLRRGNE VDLTIAMATI SELIEDVNHY INVKEQVRNQ
ILDLASKIAP GYNVRVYVNT GDKIDKNILY LTVTGTSAEH GDDGMTGRGN RGVGLITPMR
PMSLEATAGK NPVNHVGKLY NVLANLIANK IAQEVKDVKF SQVQVLGQIG RPIDDPLIAN
VDVITYDGKL TDETKNEISG IVDEMLSSFN KLTELILEGK ATLF
