(data stored in SCRATCH zone)

SWISSPROT: B6H8Q7_PENRW

ID   B6H8Q7_PENRW            Unreviewed;       387 AA.
AC   B6H8Q7;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 64.
DE   RecName: Full=S-adenosylmethionine synthase {ECO:0000256|RuleBase:RU000541};
DE            EC=2.5.1.6 {ECO:0000256|RuleBase:RU000541};
GN   ORFNames=Pc16g04380 {ECO:0000313|EMBL:CAP93108.1}, PCH_Pc16g04380
GN   {ECO:0000313|EMBL:CAP93108.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP93108.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP93108.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC       methionine and ATP. {ECO:0000256|RuleBase:RU000541}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate +
CC       diphosphate + S-adenosyl-L-methionine.
CC       {ECO:0000256|RuleBase:RU000541}.
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|RuleBase:RU000541};
CC       Note=Binds 1 potassium ion per subunit. The potassium ion
CC       interacts primarily with the substrate.
CC       {ECO:0000256|RuleBase:RU000541};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU000541};
CC       Note=Binds 2 magnesium ions per subunit. The magnesium ions
CC       interact primarily with the substrate.
CC       {ECO:0000256|RuleBase:RU000541};
CC   -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine
CC       biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
CC       {ECO:0000256|RuleBase:RU000541}.
CC   -!- SIMILARITY: Belongs to the AdoMet synthase family.
CC       {ECO:0000256|RuleBase:RU004462}.
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DR   EMBL; AM920431; CAP93108.1; -; Genomic_DNA.
DR   RefSeq; XP_002560790.1; XM_002560744.1.
DR   STRING; 500485.XP_002560790.1; -.
DR   EnsemblFungi; CAP93108; CAP93108; PCH_Pc16g04380.
DR   GeneID; 8304531; -.
DR   KEGG; pcs:Pc16g04380; -.
DR   eggNOG; KOG1506; Eukaryota.
DR   eggNOG; COG0192; LUCA.
DR   HOGENOM; HOG000245710; -.
DR   KO; K00789; -.
DR   OMA; PGHFLFT; -.
DR   OrthoDB; EOG092C2SCC; -.
DR   BioCyc; PCHR:PC16G04380-MONOMER; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000000724; Contig Pc00c16.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
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; B6H8Q7.
DR   SWISS-2DPAGE; B6H8Q7.
KW   ATP-binding {ECO:0000256|RuleBase:RU000541};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Magnesium {ECO:0000256|RuleBase:RU000541};
KW   Metal-binding {ECO:0000256|RuleBase:RU000541};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000541};
KW   One-carbon metabolism {ECO:0000256|RuleBase:RU000541};
KW   Potassium {ECO:0000256|RuleBase:RU000541};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transferase {ECO:0000256|RuleBase:RU000541}.
FT   DOMAIN       10    107       S-AdoMet_synt_N. {ECO:0000259|Pfam:
FT                                PF00438}.
FT   DOMAIN      122    242       S-AdoMet_synt_M. {ECO:0000259|Pfam:
FT                                PF02772}.
FT   DOMAIN      244    380       S-AdoMet_synt_C. {ECO:0000259|Pfam:
FT                                PF02773}.
SQ   SEQUENCE   387 AA;  42179 MW;  DA915D6A88724B2D CRC64;
     MGSVSNSGTF LFTSESVGEG HPDKIADQVS DAILDACLAE DPLSKVACET ATKTGMIMVF
     GEITTKARLD YQKIIRGAIK DIGYDASEKG FDYKTCNVLV AIEQQSPDIA QGLHYEEALE
     KLGAGDQGIM FGYATDETPE LLPLTVLFSH KLNAAMKAAR QDGSIPWLLP DTKTQVTIEY
     AHDNGAVKPL RVDTVVVSAQ HTDDVSTEEL RAVIKEKIVR KVIPAELLDD RTVYHIQPSG
     RFVIGGPQGD AGLTGRKIIV DTYGGWGAHG GGAFSGKDYS KVDRSAAYVA RWIAKSLVNA
     KLARRALVQL SYAIGVAEPL SIFVETYGTS SKTSDELVQI IRNNFDLRPG VIVKDLDLAK
     PIYYQTAKNG HFTNQEFSWE SPRTLKF
//

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