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METK_PYRAB
ID   METK_PYRAB              Reviewed;         401 AA.
AC   Q9V1P7; G8ZI14;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=S-adenosylmethionine synthase;
DE            Short=AdoMet synthase;
DE            EC=2.5.1.6;
DE   AltName: Full=Methionine adenosyltransferase;
GN   Name=mat; OrderedLocusNames=PYRAB03800; ORFNames=PAB2094;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
CC   -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC       methionine and ATP. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC       S-adenosyl-L-methionine from L-methionine: step 1/1.
CC   -!- SIMILARITY: Belongs to the AdoMet synthase 2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB49302.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CCE69757.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ248284; CAB49302.1; ALT_INIT; Genomic_DNA.
DR   EMBL; HE613800; CCE69757.1; ALT_INIT; Genomic_DNA.
DR   PIR; G75152; G75152.
DR   RefSeq; WP_048146541.1; NC_000868.1.
DR   AlphaFoldDB; Q9V1P7; -.
DR   SMR; Q9V1P7; -.
DR   STRING; 272844.PAB2094; -.
DR   PRIDE; Q9V1P7; -.
DR   EnsemblBacteria; CAB49302; CAB49302; PAB2094.
DR   GeneID; 1495270; -.
DR   KEGG; pab:PAB2094; -.
DR   PATRIC; fig|272844.11.peg.400; -.
DR   eggNOG; arCOG01678; Archaea.
DR   HOGENOM; CLU_057642_0_0_2; -.
DR   OMA; IGHPDSI; -.
DR   OrthoDB; 21658at2157; -.
DR   PhylomeDB; Q9V1P7; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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   3: Inferred from homology;
KW   ATP-binding; Magnesium; Nucleotide-binding; One-carbon metabolism;
KW   Transferase.
FT   CHAIN           1..401
FT                   /note="S-adenosylmethionine synthase"
FT                   /id="PRO_0000150035"
FT   BINDING         136..141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   401 AA;  44189 MW;  77B31C049E31D3BA CRC64;
     MARNIVVEEI VRTPVEKQKV ELVERKGIGH PDSIADGIAE SISRALSREY MKRYGVILHH
     NTDQVEVVGG RAYPRFGGGE VVKPIYILLS GRAVELVDQE LFPVHEVAIK AAKEYLKKNI
     RHLDVENHVV IDSRIGQGSV DLVSVFNKAK ENPIPLANDT SFGVGFAPLT ETERLVYETE
     RLLNGEKFKK ELPAVGEDIK VMGLRRGDEI DLTIAAAIVD SEVSGPKEYL EVKEKIAEAV
     EELAKDITSR KVNIYVNTAD DPDSGIFYIT VTGTSAEAGD DGSVGRGNRV NGLITPNRHM
     SMEAAAGKNP VSHVGKIYNI LAMFIANDIA KTLPVEEVYV RILSQIGKPI DQPLVASIQV
     IPKQGHSVKE FEKDAYSIAD EWLANITKIQ KMILEDKISV F
 
 
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