(data stored in SCRATCH zone)

SWISSPROT: C8W5Z8_DESAS

ID   C8W5Z8_DESAS            Unreviewed;       393 AA.
AC   C8W5Z8;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   16-JAN-2019, entry version 67.
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=Dtox_0533 {ECO:0000313|EMBL:ACV61453.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61453.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61453.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00086}.
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DR   EMBL; CP001720; ACV61453.1; -; Genomic_DNA.
DR   RefSeq; WP_015756172.1; NC_013216.1.
DR   STRING; 485916.Dtox_0533; -.
DR   EnsemblBacteria; ACV61453; ACV61453; Dtox_0533.
DR   KEGG; dae:Dtox_0533; -.
DR   eggNOG; ENOG4105CPH; Bacteria.
DR   eggNOG; COG0192; LUCA.
DR   HOGENOM; HOG000245710; -.
DR   OrthoDB; 1024388at2; -.
DR   BioCyc; DACE485916:G1GFV-539-MONOMER; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000002217; 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; C8W5Z8.
DR   SWISS-2DPAGE; C8W5Z8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00086};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
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:UP000002217};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00086,
KW   ECO:0000313|EMBL:ACV61453.1}.
FT   DOMAIN        4    101       S-AdoMet_synt_N. {ECO:0000259|Pfam:
FT                                PF00438}.
FT   DOMAIN      124    241       S-AdoMet_synt_M. {ECO:0000259|Pfam:
FT                                PF02772}.
FT   DOMAIN      243    382       S-AdoMet_synt_C. {ECO:0000259|Pfam:
FT                                PF02773}.
FT   NP_BIND     173    175       ATP. {ECO:0000256|HAMAP-Rule:MF_00086}.
FT   NP_BIND     255    256       ATP. {ECO:0000256|HAMAP-Rule:MF_00086}.
FT   REGION       99    109       Flexible loop. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
FT   METAL        17     17       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
FT   METAL        43     43       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
FT   BINDING      15     15       ATP. {ECO:0000256|HAMAP-Rule:MF_00086}.
FT   BINDING      56     56       Methionine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
FT   BINDING      99     99       Methionine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
FT   BINDING     249    249       ATP; shared with neighboring subunit.
FT                                {ECO:0000256|HAMAP-Rule:MF_00086}.
FT   BINDING     249    249       Methionine; shared with neighboring
FT                                subunit. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
FT   BINDING     272    272       ATP; via amide nitrogen; shared with
FT                                neighboring subunit. {ECO:0000256|HAMAP-
FT                                Rule:MF_00086}.
FT   BINDING     276    276       ATP; shared with neighboring subunit.
FT                                {ECO:0000256|HAMAP-Rule:MF_00086}.
FT   BINDING     280    280       Methionine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
SQ   SEQUENCE   393 AA;  42889 MW;  C2E79B75787ADE35 CRC64;
     MRNRVFTSES VTEGHPDKLC DQISDAVLDN ILEQDKNARV ACECVATTGM VLVTGEITSS
     CYVDIPSIVR QTVQNIGYDN PEYGFDYKAC AVLTSIDEQS PDIAMGVNSS YEAKKLKPDE
     ADYIGAGDQG MMFGFACDET PELMPAPISL AHKLAQRLAG VRKSGELNWL RPDGKTQVAV
     EYDDSGKILR CAAIVVSAQH NPDVSSDTLR EAIIETVIKP VIPKKYLDKD THIYVNPTGC
     FVIGGPVGDS GLTGRKIIVD TYGGYASHGG GAFSGKDPTK VDRSAAYMVR HIAKNIVAAG
     LAQRCQIEVA YAIGVSNPIS IHIDTQGTGI FSDQRLADVV RECFDLRPAR IISYLDLRNP
     IYTQTAAYGH FGRPELNLPW ERTNMAEILK QYK
//

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