ID METE_ECOL5 Reviewed; 753 AA.
AC Q0TAP6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 01-MAY-2013, entry version 56.
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=ECP_4023;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG71983.1; -; Genomic_DNA.
DR RefSeq; YP_671884.1; NC_008253.1.
DR ProteinModelPortal; Q0TAP6; -.
DR SMR; Q0TAP6; 4-752.
DR STRING; 362663.ECP_4023; -.
DR EnsemblBacteria; ABG71983; ABG71983; ECP_4023.
DR GeneID; 4188754; -.
DR KEGG; ecp:ECP_4023; -.
DR PATRIC; 18198939; VBIEscCol77757_4067.
DR eggNOG; COG0620; -.
DR HOGENOM; HOG000246221; -.
DR KO; K00549; -.
DR OMA; RNIWRAN; -.
DR PhylomeDB; Q0TAP6; -.
DR ProtClustDB; PRK05222; -.
DR BioCyc; ECOL362663:GIY5-4055-MONOMER; -.
DR UniPathway; UPA00051; UER00082.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:HAMAP.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA: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; Methionine_synth.
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_1000017241.
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; 84709 MW; E481F912ED56B6E4 CRC64;
MTILNHTLGF PRVGLRRELK KAQESYWAGN STREELLAVG RELRARHWDQ QKQAGIDLLP
VGDFAWYDHV LTTSLLLGNV PARHQNKDGS VDIDTLFRIG RGRAPTGEPA AAAEMTKWFN
TNYHYMVPEF VKGQQFKLTW TQLLEEVDEA LALGHKVKPV LLGPVTYLWL GKVKGEQFDR
LSLLNDILPV YQQVLAELAK RGIEWVQIDE PALVLELPQA WLDAYKPAYD ALQGQVKLLL
TTYFEGVTPN LDTITALPVQ GLHVDLVHGK DDVAELHKRL PSDWLLSAGL INGRNVWRAD
LTEKYAQIKD IVGKRDLWVA SSCSLLHSPI DLSVETRLDA EVKSWFAFAL QKCHELALLR
DVLNSGDTAA LAEWSAPIQA RRHSTRVHNP AVEKRLAAIT AQDSQRTNVY 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
//
