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Database: UniProt/SWISS-PROT
Entry: METE_ECO7I
LinkDB: METE_ECO7I
Original site: METE_ECO7I 
ID   METE_ECO7I              Reviewed;         753 AA.
AC   B7NV51;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   11-JUN-2014, entry version 41.
DE   RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase;
DE            EC=2.1.1.14;
DE   AltName: Full=Cobalamin-independent methionine synthase;
DE   AltName: Full=Methionine synthase, vitamin-B12 independent isozyme;
GN   Name=metE; OrderedLocusNames=ECIAI39_3180;
OS   Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI39 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A.,
RA   Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA   Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA   Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA   Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA   Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA   Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC       methyltetrahydrofolate to homocysteine resulting in methionine
CC       formation (By similarity).
CC   -!- CATALYTIC ACTIVITY: 5-methyltetrahydropteroyltri-L-glutamate + L-
CC       homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine.
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 (MetE route): step
CC       1/1.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine
CC       synthase family.
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DR   EMBL; CU928164; CAR19299.1; -; Genomic_DNA.
DR   RefSeq; YP_002409107.1; NC_011750.1.
DR   ProteinModelPortal; B7NV51; -.
DR   SMR; B7NV51; 4-752.
DR   STRING; 585057.ECIAI39_3180; -.
DR   EnsemblBacteria; CAR19299; CAR19299; ECIAI39_3180.
DR   GeneID; 7150135; -.
DR   KEGG; ect:ECIAI39_3180; -.
DR   PATRIC; 18335223; VBIEscCol51957_3301.
DR   eggNOG; COG0620; -.
DR   HOGENOM; HOG000246221; -.
DR   KO; K00549; -.
DR   OMA; FKANPAH; -.
DR   OrthoDB; EOG6FFS3G; -.
DR   BioCyc; ECOL585057:GJ8I-3302-MONOMER; -.
DR   UniPathway; UPA00051; UER00082.
DR   GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00172; Meth_synth; 1.
DR   InterPro; IPR013215; Cbl-indep_Met_Synth_N.
DR   InterPro; IPR006276; Cobalamin-indep_Met_synthase.
DR   InterPro; IPR002629; Met_Synth_C/arc.
DR   Pfam; PF08267; Meth_synt_1; 1.
DR   Pfam; PF01717; Meth_synt_2; 1.
DR   PIRSF; PIRSF000382; MeTrfase_B12_ind; 1.
DR   TIGRFAMs; TIGR01371; met_syn_B12ind; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Metal-binding;
KW   Methionine biosynthesis; Methyltransferase; Repeat; Transferase; Zinc.
FT   CHAIN         1    753       5-methyltetrahydropteroyltriglutamate--
FT                                homocysteine methyltransferase.
FT                                /FTId=PRO_1000191200.
FT   METAL       641    641       Zinc (By similarity).
FT   METAL       643    643       Zinc (By similarity).
FT   METAL       726    726       Zinc (By similarity).
SQ   SEQUENCE   753 AA;  84592 MW;  4DB09AE1FA60905C CRC64;
     MTILNHTLGF PRVGLRRELK KAQESYWAGN STREELLAVG RELRARHWDQ QKQAGIDLLP
     VGDFAWYDHV LTTSLLLGNV PARHQNNDGS VDIDTLFRIG RGRAPTGEPA AAAEMTKWFN
     TNYHYMVPEF VKGQQFKLTW TQLLEEVDEA LALGHKVKPV LLGPVTYLWL GKVKGEQFDR
     LSLLNDILPV YQQVLAELAK RGIEWVQIDE PALVLELPQA WLDAYKPAYD ALQGQVKLLL
     TTYFEGVTPN LDTITALPVQ GLHVDLVHGK DDVAELHKRL PSEWLLSAGL INGRNVWRAD
     LTEKYAQIKD IVGKRDLWVA SSCSLLHSPI DLSVETRLDA EVKSWFAFAL QKCHELALLR
     DALNSGDTAA LAAWSAPIQA RRHSTRVHNP AVEKRLAAIT AQDSQRANVY EVRAEAQRAR
     FKLPAWPTTT IGSFPQTTEI RTLRLDFKKG NLDANNYRTG IAEHIKQAIV EQERLGLDVL
     VHGEAERNDM VEYFGEHLDG FVFTQNGWVQ SYGSRCVKPP IVIGDVSRPA PITVEWAKYA
     QSLTDKPVKG MLTGPVTILC WSFPREDVSR ETIAKQIALA LRDEVADLEA AGIGIIQIDE
     PALREGLPLR RSDWDAYLQW GVEAFRINAA VAKDDTQIHT HMCYCEFNDI MDSIAALDAD
     VITIETSRSD MELLESFEEF DYPNEIGPGV YDIHSPNVPS VEWIEALLKK AAKRIPAERL
     WVNPDCGLKT RGWPETRAAL ANMVQAAQNL RRG
//
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