(data stored in ACNUC7421 zone)

SWISSPROT: A4ATS4_MARSH

ID   A4ATS4_MARSH            Unreviewed;       418 AA.
AC   A4ATS4;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   RecName: Full=S-adenosylmethionine synthase {ECO:0000256|HAMAP-Rule:MF_00086};
DE            Short=AdoMet synthase {ECO:0000256|HAMAP-Rule:MF_00086};
DE            EC=2.5.1.6 {ECO:0000256|HAMAP-Rule:MF_00086};
DE   AltName: Full=MAT {ECO:0000256|HAMAP-Rule:MF_00086};
DE   AltName: Full=Methionine adenosyltransferase {ECO:0000256|HAMAP-Rule:MF_00086};
GN   Name=metK {ECO:0000256|HAMAP-Rule:MF_00086};
GN   OrderedLocusNames=FB2170_17206 {ECO:0000313|EMBL:EAR00844.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00844.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00844.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet)
CC       from methionine and ATP. The overall synthetic reaction is
CC       composed of two sequential steps, AdoMet formation and the
CC       subsequent tripolyphosphate hydrolysis which occurs prior to
CC       release of AdoMet from the enzyme. {ECO:0000256|HAMAP-
CC       Rule:MF_00086}.
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:0000256|HAMAP-Rule:MF_00086};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00086};
CC       Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00086};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00086};
CC       Note=Binds 2 divalent ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00086};
CC   -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine
CC       biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00086}.
CC   -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000256|HAMAP-
CC       Rule:MF_00086}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00086,
CC       ECO:0000256|RuleBase:RU000542}.
CC   -!- SIMILARITY: Belongs to the AdoMet synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00086, ECO:0000256|RuleBase:RU004462}.
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DR   EMBL; CP002157; EAR00844.1; -; Genomic_DNA.
DR   RefSeq; WP_013304647.1; NC_014472.1.
DR   STRING; 313603.FB2170_17206; -.
DR   EnsemblBacteria; EAR00844; EAR00844; FB2170_17206.
DR   KEGG; fbc:FB2170_17206; -.
DR   eggNOG; ENOG4105CPH; Bacteria.
DR   eggNOG; COG0192; LUCA.
DR   HOGENOM; HOG000245710; -.
DR   KO; K00789; -.
DR   OMA; MPYLRPD; -.
DR   OrthoDB; 1024388at2; -.
DR   BioCyc; MSP313603:G1GNS-217-MONOMER; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   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   3: Inferred from homology;
DR   PRODOM; A4ATS4.
DR   SWISS-2DPAGE; A4ATS4.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00086};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00086};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00086,
KW   ECO:0000256|RuleBase:RU000542};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00086,
KW   ECO:0000256|RuleBase:RU000542};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00086};
KW   One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00086};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_00086,
KW   ECO:0000256|RuleBase:RU000542};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00086}.
FT   DOMAIN        3     99       S-AdoMet_synt_N. {ECO:0000259|Pfam:
FT                                PF00438}.
FT   DOMAIN      113    243       S-AdoMet_synt_M. {ECO:0000259|Pfam:
FT                                PF02772}.
FT   DOMAIN      245    378       S-AdoMet_synt_C. {ECO:0000259|Pfam:
FT                                PF02773}.
FT   NP_BIND     164    166       ATP. {ECO:0000256|HAMAP-Rule:MF_00086}.
FT   NP_BIND     242    243       ATP. {ECO:0000256|HAMAP-Rule:MF_00086}.
FT   NP_BIND     257    258       ATP. {ECO:0000256|HAMAP-Rule:MF_00086}.
FT   REGION       98    108       Flexible loop. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
FT   METAL        16     16       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
FT   METAL        42     42       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
FT   BINDING      14     14       ATP. {ECO:0000256|HAMAP-Rule:MF_00086}.
FT   BINDING      55     55       Methionine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
FT   BINDING      98     98       Methionine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
FT   BINDING     251    251       ATP; shared with neighboring subunit.
FT                                {ECO:0000256|HAMAP-Rule:MF_00086}.
FT   BINDING     251    251       Methionine; shared with neighboring
FT                                subunit. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
FT   BINDING     274    274       ATP; via amide nitrogen; shared with
FT                                neighboring subunit. {ECO:0000256|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING     278    278       ATP; shared with neighboring subunit.
FT                                {ECO:0000256|HAMAP-Rule:MF_00086}.
FT   BINDING     282    282       Methionine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
SQ   SEQUENCE   418 AA;  45938 MW;  0F55FE49B2D1C202 CRC64;
     MAYLFTSESV SEGHPDKVAD QISDALLDSF LAFDPESKVA CETLVTTGQV VLAGEVKSHT
     YLDVQNIARN VINKIGYTKG EYQFSGDSCG VISLIHEQSQ DINQGVDRGS KEEQGAGDQG
     MMFGYATKET ENYMPLALDI SHRILQTLAD LRREGNEIAY LRPDAKAQVT IEYSDDNVPQ
     RIDTIVVSTQ HDQFDANDDK MLAKIKDDII SILIPLVVNQ LPSNMQTLFD DQIKYHINPT
     GKFVIGGPHG DTGLTGRKII VDTYGGKGAH GGGAFSGKDP SKVDRSAAYA ARHIAKNLVA
     AGISDEVLVQ VSYAIGVVEP TSIFVNTYGT SKVDKSDGEI AEIVSQLFDM RPFAIEERLK
     LRNPIYLETA AYGHMGKEPK VITKVFESPY NGRIETEVEL FTWEKLDMVD EVKAAFKI
//

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