METE_ECOLI
ID METE_ECOLI Reviewed; 753 AA.
AC P25665; Q2M8D4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 6.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00172};
DE EC=2.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00172};
DE AltName: Full=Cobalamin-independent methionine synthase {ECO:0000255|HAMAP-Rule:MF_00172};
DE AltName: Full=Methionine synthase, vitamin-B12 independent isozyme {ECO:0000255|HAMAP-Rule:MF_00172};
GN Name=metE {ECO:0000255|HAMAP-Rule:MF_00172};
GN OrderedLocusNames=b3829, JW3805;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=1339288; DOI=10.1021/bi00141a013;
RA Gonzalez J.C., Banerjee R.V., Huang S., Sumner J.S., Matthews R.G.;
RT "Comparison of cobalamin-independent and cobalamin-dependent methionine
RT synthases from Escherichia coli: two solutions to the same chemical
RT problem.";
RL Biochemistry 31:6045-6056(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 604
RP AND 658.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX PubMed=2643109; DOI=10.1073/pnas.86.1.85;
RA Maxon M.E., Redfield B., Cai X.-Y., Shoeman R., Fujita K., Fisher W.,
RA Stauffer G., Weissbach H., Brot N.;
RT "Regulation of methionine synthesis in Escherichia coli: effect of the MetR
RT protein on the expression of the metE and metR genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:85-89(1989).
RN [7]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [8]
RP CHARACTERIZATION, AND MUTAGENESIS OF CYS-726.
RX PubMed=8823155; DOI=10.1021/bi9615452;
RA Gonzalez J.C., Peariso K., Penner-Hahn J.E., Matthews R.G.;
RT "Cobalamin-independent methionine synthase from Escherichia coli: a zinc
RT metalloenzyme.";
RL Biochemistry 35:12228-12234(1996).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP MUTAGENESIS OF HIS-641; CYS-643 AND CYS-726.
RX PubMed=10625458; DOI=10.1021/bi992062b;
RA Zhou Z.S., Peariso K., Penner-Hahn J.E., Matthews R.G.;
RT "Identification of the zinc ligands in cobalamin-independent methionine
RT synthase (MetE) from Escherichia coli.";
RL Biochemistry 38:15915-15926(1999).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC methyltetrahydrofolate to homocysteine resulting in methionine
CC formation. {ECO:0000255|HAMAP-Rule:MF_00172}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-
CC methionine + tetrahydropteroyltri-L-glutamate; Xref=Rhea:RHEA:21196,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, ChEBI:CHEBI:58199,
CC ChEBI:CHEBI:58207; EC=2.1.1.14; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00172};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00172};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00172};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00172}.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P25665; P03018: uvrD; NbExp=2; IntAct=EBI-551247, EBI-559573;
CC -!- MISCELLANEOUS: Has an absolute requirement for a polyglutamylated
CC folate as substrate. Its activity depends on phosphate anions and
CC divalent cations.
CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC family. {ECO:0000255|HAMAP-Rule:MF_00172, ECO:0000305}.
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DR EMBL; M87625; AAA23544.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67625.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76832.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77472.1; -; Genomic_DNA.
DR EMBL; J04155; AAA24160.1; -; Genomic_DNA.
DR PIR; F65187; A42863.
DR RefSeq; NP_418273.1; NC_000913.3.
DR RefSeq; WP_000153907.1; NZ_SSZK01000046.1.
DR AlphaFoldDB; P25665; -.
DR SMR; P25665; -.
DR BioGRID; 4259477; 17.
DR BioGRID; 852620; 1.
DR DIP; DIP-6847N; -.
DR IntAct; P25665; 12.
DR STRING; 511145.b3829; -.
DR jPOST; P25665; -.
DR PaxDb; P25665; -.
DR PRIDE; P25665; -.
DR EnsemblBacteria; AAC76832; AAC76832; b3829.
DR EnsemblBacteria; BAE77472; BAE77472; BAE77472.
DR GeneID; 948323; -.
DR KEGG; ecj:JW3805; -.
DR KEGG; eco:b3829; -.
DR PATRIC; fig|1411691.4.peg.2879; -.
DR EchoBASE; EB0579; -.
DR eggNOG; COG0620; Bacteria.
DR HOGENOM; CLU_013175_0_0_6; -.
DR InParanoid; P25665; -.
DR OMA; KVMKGML; -.
DR PhylomeDB; P25665; -.
DR BioCyc; EcoCyc:HOMOCYSMET-MON; -.
DR BioCyc; MetaCyc:HOMOCYSMET-MON; -.
DR BRENDA; 2.1.1.14; 2026.
DR UniPathway; UPA00051; UER00082.
DR PRO; PR:P25665; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0008705; F:methionine synthase activity; IDA:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0050667; P:homocysteine metabolic process; IDA:BHF-UCL.
DR GO; GO:0009086; P:methionine biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IDA:BHF-UCL.
DR CDD; cd03311; CIMS_C_terminal_like; 1.
DR Gene3D; 3.20.20.210; -; 2.
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 InterPro; IPR038071; UROD/MetE-like_sf.
DR Pfam; PF08267; Meth_synt_1; 1.
DR Pfam; PF01717; Meth_synt_2; 1.
DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1.
DR SUPFAM; SSF51726; SSF51726; 2.
DR TIGRFAMs; TIGR01371; met_syn_B12ind; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Direct protein sequencing; Metal-binding;
KW Methionine biosynthesis; Methyltransferase; Reference proteome; Repeat;
KW Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..753
FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT methyltransferase"
FT /id="PRO_0000098630"
FT ACT_SITE 694
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 17..20
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 117
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 431..433
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 431..433
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 484
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 484
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 515..516
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 561
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 599
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 599
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 605
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 641
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 643
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 665
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT BINDING 726
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172"
FT MUTAGEN 641
FT /note="H->N: Impaired activity, lower affinity for zinc
FT binding."
FT /evidence="ECO:0000269|PubMed:10625458"
FT MUTAGEN 641
FT /note="H->Q: Impaired activity, lower affinity for zinc
FT binding. Binds homocysteine 2-4x more weakly than wild-
FT type."
FT /evidence="ECO:0000269|PubMed:10625458"
FT MUTAGEN 643
FT /note="C->S: Impaired activity, lower affinity for zinc
FT binding. Binds homocysteine 7x tighter than wild-type."
FT /evidence="ECO:0000269|PubMed:10625458"
FT MUTAGEN 726
FT /note="C->S: Impaired activity, lower affinity for zinc
FT binding. Binds homocysteine 2-4x more weakly than wild-
FT type."
FT /evidence="ECO:0000269|PubMed:10625458,
FT ECO:0000269|PubMed:8823155"
FT CONFLICT 363
FT /note="L -> V (in Ref. 1; AAA23544)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="E -> Q (in Ref. 3; AAA67625)"
FT /evidence="ECO:0000305"
FT CONFLICT 659
FT /note="A -> R (in Ref. 3; AAA67625)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 753 AA; 84674 MW; C46BE52F227AFAF1 CRC64;
MTILNHTLGF PRVGLRRELK KAQESYWAGN STREELLAVG RELRARHWDQ QKQAGIDLLP
VGDFAWYDHV LTTSLLLGNV PARHQNKDGS VDIDTLFRIG RGRAPTGEPA AAAEMTKWFN
TNYHYMVPEF VKGQQFKLTW TQLLDEVDEA LALGHKVKPV LLGPVTWLWL GKVKGEQFDR
LSLLNDILPV YQQVLAELAK RGIEWVQIDE PALVLELPQA WLDAYKPAYD ALQGQVKLLL
TTYFEGVTPN LDTITALPVQ GLHVDLVHGK DDVAELHKRL PSDWLLSAGL INGRNVWRAD
LTEKYAQIKD IVGKRDLWVA SSCSLLHSPI DLSVETRLDA EVKSWFAFAL QKCHELALLR
DALNSGDTAA LAEWSAPIQA RRHSTRVHNP AVEKRLAAIT AQDSQRANVY EVRAEAQRAR
FKLPAWPTTT IGSFPQTTEI RTLRLDFKKG NLDANNYRTG IAEHIKQAIV EQERLGLDVL
VHGEAERNDM VEYFGEHLDG FVFTQNGWVQ SYGSRCVKPP IVIGDISRPA PITVEWAKYA
QSLTDKPVKG MLTGPVTILC WSFPREDVSR ETIAKQIALA LRDEVADLEA AGIGIIQIDE
PALREGLPLR RSDWDAYLQW GVEAFRINAA VAKDDTQIHT HMCYCEFNDI MDSIAALDAD
VITIETSRSD MELLESFEEF DYPNEIGPGV YDIHSPNVPS VEWIEALLKK AAKRIPAERL
WVNPDCGLKT RGWPETRAAL ANMVQAAQNL RRG
