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Database: UniProt
Entry: P37586
LinkDB: P37586
Original site: P37586 
ID   METH_SALTY              Reviewed;        1227 AA.
AC   P37586;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   09-JUL-2014, entry version 115.
DE   RecName: Full=Methionine synthase;
DE            EC=2.1.1.13;
DE   AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase;
DE   AltName: Full=Methionine synthase, vitamin-B12 dependent;
DE            Short=MS;
GN   Name=metH; OrderedLocusNames=STM4188;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-371.
RC   STRAIN=LT2;
RX   PubMed=3072256; DOI=10.1016/0378-1119(88)90325-3;
RA   Urbanowski M.L., Stauffer G.V.;
RT   "The control region of the metH gene of Salmonella typhimurium LT2: an
RT   atypical met promoter.";
RL   Gene 73:193-200(1988).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from methyl-
CC       cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and
CC       methionine. Subsequently, remethylates the cofactor using
CC       methyltetrahydrofolate (By similarity).
CC   -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + L-homocysteine =
CC       tetrahydrofolate + L-methionine.
CC   -!- COFACTOR: Methylcobalamin (MeCBL) (By similarity).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-methionine from L-homocysteine (MetH route): step
CC       1/1.
CC   -!- DOMAIN: Modular enzyme with four functionally distinct domains.
CC       The isolated Hcy-binding domain catalyzes methyl transfer from
CC       free methylcobalamin to homocysteine. The Hcy-binding domain in
CC       association with the pterin-binding domain catalyzes the
CC       methylation of cob(I)alamin by methyltetrahydrofolate and the
CC       methylation of homocysteine. The B12-binding domain binds the
CC       cofactor. The AdoMet activation domain binds S-adenosyl-L-
CC       methionine. Under aerobic conditions cob(I)alamin can be converted
CC       to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-
CC       methionine and flavodoxin regenerates methylcobalamin (By
CC       similarity).
CC   -!- MISCELLANEOUS: L-homocysteine is bound via the zinc atom (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine
CC       synthase family.
CC   -!- SIMILARITY: Contains 1 AdoMet activation domain.
CC   -!- SIMILARITY: Contains 1 B12-binding domain.
CC   -!- SIMILARITY: Contains 1 B12-binding N-terminal domain.
CC   -!- SIMILARITY: Contains 1 Hcy-binding domain.
CC   -!- SIMILARITY: Contains 1 pterin-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL23012.1; Type=Erroneous initiation;
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DR   EMBL; AE006468; AAL23012.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_463053.2; NC_003197.1.
DR   ProteinModelPortal; P37586; -.
DR   SMR; P37586; 651-1227.
DR   STRING; 99287.STM4188.S; -.
DR   PaxDb; P37586; -.
DR   PRIDE; P37586; -.
DR   EnsemblBacteria; AAL23012; AAL23012; STM4188.
DR   GeneID; 1255714; -.
DR   KEGG; stm:STM4188.S; -.
DR   PATRIC; 32387269; VBISalEnt20916_4402.
DR   eggNOG; COG1410; -.
DR   KO; K00548; -.
DR   OMA; LTEHYAM; -.
DR   OrthoDB; EOG6091CH; -.
DR   PhylomeDB; P37586; -.
DR   BioCyc; SENT99287:GCTI-4218-MONOMER; -.
DR   UniPathway; UPA00051; UER00081.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1240.10; -; 1.
DR   Gene3D; 3.10.196.10; -; 1.
DR   Gene3D; 3.20.20.20; -; 1.
DR   Gene3D; 3.20.20.330; -; 1.
DR   Gene3D; 3.40.50.280; -; 1.
DR   InterPro; IPR003759; Cbl-bd_cap.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
DR   InterPro; IPR011822; MetH.
DR   InterPro; IPR000489; Pterin-binding.
DR   InterPro; IPR003726; S_MeTrfase.
DR   InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF02607; B12-binding_2; 1.
DR   Pfam; PF02965; Met_synt_B12; 1.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   Pfam; PF02574; S-methyl_trans; 1.
DR   PIRSF; PIRSF000381; MetH; 1.
DR   SMART; SM01018; B12-binding_2; 1.
DR   SUPFAM; SSF47644; SSF47644; 1.
DR   SUPFAM; SSF51717; SSF51717; 1.
DR   SUPFAM; SSF52242; SSF52242; 1.
DR   SUPFAM; SSF56507; SSF56507; 1.
DR   SUPFAM; SSF82282; SSF82282; 1.
DR   TIGRFAMs; TIGR02082; metH; 1.
DR   PROSITE; PS50974; ADOMET_ACTIVATION; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS51337; B12_BINDING_NTER; 1.
DR   PROSITE; PS50970; HCY; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome;
KW   Metal-binding; Methionine biosynthesis; Methyltransferase;
KW   Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase;
KW   Zinc.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1227       Methionine synthase.
FT                                /FTId=PRO_0000204536.
FT   DOMAIN        2    325       Hcy-binding.
FT   DOMAIN      356    617       Pterin-binding.
FT   DOMAIN      650    744       B12-binding N-terminal.
FT   DOMAIN      746    881       B12-binding.
FT   DOMAIN      897   1227       AdoMet activation.
FT   REGION      834    835       Cobalamin-binding (By similarity).
FT   REGION     1189   1190       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   METAL       247    247       Zinc (By similarity).
FT   METAL       310    310       Zinc (By similarity).
FT   METAL       311    311       Zinc (By similarity).
FT   METAL       759    759       Cobalt (cobalamin axial ligand) (By
FT                                similarity).
FT   BINDING     804    804       Cobalamin (By similarity).
FT   BINDING     946    946       S-adenosyl-L-methionine (By similarity).
FT   BINDING    1134   1134       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING    1138   1138       Cobalamin; via carbonyl oxygen (By
FT                                similarity).
FT   CONFLICT    115    115       A -> R (in Ref. 2).
SQ   SEQUENCE   1227 AA;  136004 MW;  11C8E21745FF5354 CRC64;
     MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLHEEDFRGE RFADWPCDLK GNNDLLVLSK
     PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYRMESLS AEINYAAAKL ARACADEWTA
     RTPEKPRFVA GVLGPTNRTA SISPDVNDPA FRNITFDQLV AAYRESTKAL VEGGADLILI
     ETVFDTLNAK AAVFAVKEEF EALGVDLPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA
     LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAE
     AGFLNIVGGC CGTTPEHIAA MSRAVAGLLP RQLPDIPVAC RLSGLEPLNI GDDSLFVNVG
     ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VESGAQIIDI NMDEGMLDAE AAMVRFLSLI
     AGEPDIARVP IMIDSSKWEV IEKGLKCIQG KGIVNSISMK EGVEAFIHHA KLLRRYGAAV
     VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ
     DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG
     QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLDLAEKYRG SKTDEAANAQ QAEWRSWDVK
     KRLEYSLVKG ITEFIEQDTE EARQQAARPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK
     SARVMKQAVA YLEPFIEASK EKGSSNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL
     GVMVPAEKIL RTAREVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA
     HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHARKKPR
     TPPVTLEAAR DNDLAFDWER YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY
     PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KLLNPRGVVG LFPANRVGDD IEIYRDETRT
     HVLTVSHHLR QQTEKVGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH
     DDYNKIMVKA IADRLAEAFA EYLHERVRKV YWGYAPNESL SNDELIRENY QGIRPAPGYP
     ACPEHTEKGT IWQLLDVEKH TGMKLTESFA MWPGASVSGW YFSHPESKYF AVAQIQRDQV
     TDYAFRKGMS VEDVERWLAP NLGYDAD
//
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