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S-adenosylmethionine synthase (AdoMet synthase) (EC 2.5.1.6) (MAT) (Methionine adenosyltransferase)

 F7XUB4_MIDMI            Unreviewed;       376 AA.
F7XUB4;
21-SEP-2011, integrated into UniProtKB/TrEMBL.
21-SEP-2011, sequence version 1.
07-JUN-2017, entry version 44.
RecName: Full=S-adenosylmethionine synthase {ECO:0000256|HAMAP-Rule:MF_00086};
Short=AdoMet synthase {ECO:0000256|HAMAP-Rule:MF_00086};
EC=2.5.1.6 {ECO:0000256|HAMAP-Rule:MF_00086};
AltName: Full=MAT {ECO:0000256|HAMAP-Rule:MF_00086};
AltName: Full=Methionine adenosyltransferase {ECO:0000256|HAMAP-Rule:MF_00086};
Name=metK {ECO:0000256|HAMAP-Rule:MF_00086,
ECO:0000313|EMBL:AEI89473.1};
OrderedLocusNames=midi_01197 {ECO:0000313|EMBL:AEI89473.1};
Midichloria mitochondrii (strain IricVA).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Candidatus Midichloriaceae; Candidatus Midichloria.
NCBI_TaxID=696127 {ECO:0000313|EMBL:AEI89473.1, ECO:0000313|Proteomes:UP000006639};
[1] {ECO:0000313|EMBL:AEI89473.1, ECO:0000313|Proteomes:UP000006639}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IricVA {ECO:0000313|EMBL:AEI89473.1,
ECO:0000313|Proteomes:UP000006639};
PubMed=21690562; DOI=10.1093/molbev/msr159;
Sassera D., Lo N., Epis S., D'Auria G., Montagna M., Comandatore F.,
Horner D., Pereto J., Luciano A.M., Franciosi F., Ferri E., Crotti E.,
Bazzocchi C., Daffonchio D., Sacchi L., Moya A., Latorre A., Bandi C.;
"Phylogenomic evidence for the presence of a flagellum and cbb3
oxidase in the free-living mitochondrial ancestor.";
Mol. Biol. Evol. 28:3285-3296(2011).
-!- FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet)
from methionine and ATP. The overall synthetic reaction is
composed of two sequential steps, AdoMet formation and the
subsequent tripolyphosphate hydrolysis which occurs prior to
release of AdoMet from the enzyme. {ECO:0000256|HAMAP-
Rule:MF_00086}.
-!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate +
diphosphate + S-adenosyl-L-methionine. {ECO:0000256|HAMAP-
Rule:MF_00086}.
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000256|HAMAP-Rule:MF_00086};
Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_00086};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00086};
Note=Binds 2 divalent ions per subunit. {ECO:0000256|HAMAP-
Rule:MF_00086};
-!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine
biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_00086}.
-!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000256|HAMAP-
Rule:MF_00086}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00086,
ECO:0000256|RuleBase:RU000542}.
-!- SIMILARITY: Belongs to the AdoMet synthase family.
{ECO:0000256|HAMAP-Rule:MF_00086, ECO:0000256|RuleBase:RU004462}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00086}.
-----------------------------------------------------------------------
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EMBL; CP002130; AEI89473.1; -; Genomic_DNA.
RefSeq; WP_013951665.1; NC_015722.1.
STRING; 696127.midi_01197; -.
EnsemblBacteria; AEI89473; AEI89473; midi_01197.
KEGG; mmn:midi_01197; -.
eggNOG; ENOG4105CPH; Bacteria.
eggNOG; COG0192; LUCA.
KO; K00789; -.
OMA; QHHPEIQ; -.
OrthoDB; POG091H00IO; -.
UniPathway; UPA00315; UER00080.
Proteomes; UP000006639; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-HAMAP.
GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP.
GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
HAMAP; MF_00086; S_AdoMet_synth1; 1.
InterPro; IPR022631; ADOMET_SYNTHASE_CS.
InterPro; IPR022630; S-AdoMet_synt_C.
InterPro; IPR022629; S-AdoMet_synt_central.
InterPro; IPR022628; S-AdoMet_synt_N.
InterPro; IPR002133; S-AdoMet_synthetase.
InterPro; IPR022636; S-AdoMet_synthetase_sfam.
PANTHER; PTHR11964; PTHR11964; 1.
Pfam; PF02773; S-AdoMet_synt_C; 1.
Pfam; PF02772; S-AdoMet_synt_M; 1.
Pfam; PF00438; S-AdoMet_synt_N; 1.
PIRSF; PIRSF000497; MAT; 1.
SUPFAM; SSF55973; SSF55973; 3.
TIGRFAMs; TIGR01034; metK; 1.
PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00086};
Complete proteome {ECO:0000313|Proteomes:UP000006639};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00086};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00086,
ECO:0000256|RuleBase:RU000542};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00086,
ECO:0000256|RuleBase:RU000542};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00086};
One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00086};
Potassium {ECO:0000256|HAMAP-Rule:MF_00086,
ECO:0000256|RuleBase:RU000542};
Reference proteome {ECO:0000313|Proteomes:UP000006639};
Transferase {ECO:0000256|HAMAP-Rule:MF_00086,
ECO:0000313|EMBL:AEI89473.1}.
DOMAIN 5 100 S-AdoMet_synt_N.
{ECO:0000259|Pfam:PF00438}.
DOMAIN 115 231 S-AdoMet_synt_M.
{ECO:0000259|Pfam:PF02772}.
DOMAIN 233 369 S-AdoMet_synt_C.
{ECO:0000259|Pfam:PF02773}.
NP_BIND 164 166 ATP. {ECO:0000256|HAMAP-Rule:MF_00086}.
NP_BIND 245 246 ATP. {ECO:0000256|HAMAP-Rule:MF_00086}.
REGION 99 109 Flexible loop. {ECO:0000256|HAMAP-
Rule:MF_00086}.
METAL 17 17 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00086}.
METAL 43 43 Potassium. {ECO:0000256|HAMAP-
Rule:MF_00086}.
BINDING 15 15 ATP. {ECO:0000256|HAMAP-Rule:MF_00086}.
BINDING 56 56 Methionine. {ECO:0000256|HAMAP-
Rule:MF_00086}.
BINDING 99 99 Methionine. {ECO:0000256|HAMAP-
Rule:MF_00086}.
BINDING 239 239 ATP; shared with neighboring subunit.
{ECO:0000256|HAMAP-Rule:MF_00086}.
BINDING 239 239 Methionine; shared with neighboring
subunit. {ECO:0000256|HAMAP-
Rule:MF_00086}.
BINDING 262 262 ATP; via amide nitrogen; shared with
neighboring subunit. {ECO:0000256|HAMAP-
Rule:MF_00086}.
BINDING 266 266 ATP; shared with neighboring subunit.
{ECO:0000256|HAMAP-Rule:MF_00086}.
BINDING 270 270 Methionine. {ECO:0000256|HAMAP-
Rule:MF_00086}.
SEQUENCE 376 AA; 41338 MW; E5FCFA06C79E059B CRC64;
MPLRLFSSES VSEGHPDKIA DQVSDAILDA IIALDHNARV ACEVLVKNSI ILVAGEITTI
AWIDIEKTVK NVIASIGYND PELGFDARSC SPISAIGQQS HDIALGVNSK AGKELGAGDQ
GMMFGFACDE TEALMPLPIY YAHQLMQRQA EVRHKKILPW LRPDAKAQIT AKYENDRPIS
IETIVFSTQH SVGVSHKQIT EGVIEEIIRP VIPPHLLHKD TKFLINPTGY FIIGGPVADC
GLTGRKTIVD TYGGAARHGG GAFSGKDPTK VDRSAAYMAR HVAKNIVATG LASRCEIQIA
YAIGVTEPVA MYVNCFNTNK IPEEEILQLI KEKFDFRPAQ IIDYLKLRRP IYRATANYGH
FGRSGFNWED WNNVLA


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