METE_STRMU
ID METE_STRMU Reviewed; 745 AA.
AC Q8CWX6;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00172, ECO:0000303|PubMed:21840320};
DE EC=2.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00172, ECO:0000269|PubMed:21840320};
DE AltName: Full=Cobalamin-independent methionine synthase {ECO:0000255|HAMAP-Rule:MF_00172, ECO:0000303|PubMed:21840320};
DE AltName: Full=Methionine synthase, vitamin-B12 independent isozyme {ECO:0000255|HAMAP-Rule:MF_00172};
GN Name=metE {ECO:0000255|HAMAP-Rule:MF_00172, ECO:0000303|PubMed:21840320};
GN OrderedLocusNames=SMU_873;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [2] {ECO:0007744|PDB:2NQ5}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-745.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of methyltransferase from Streptococcus mutans.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [3] {ECO:0007744|PDB:3L7R, ECO:0007744|PDB:3T0C}
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) IN COMPLEXES WITH ZINC, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=21840320; DOI=10.1016/j.jmb.2011.08.005;
RA Fu T.M., Almqvist J., Liang Y.H., Li L., Huang Y., Su X.D.;
RT "Crystal structures of cobalamin-independent methionine synthase (MetE)
RT from Streptococcus mutans: a dynamic zinc-inversion model.";
RL J. Mol. Biol. 412:688-697(2011).
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 ECO:0000269|PubMed:21840320}.
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, ECO:0000269|PubMed:21840320};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00172,
CC ECO:0000269|PubMed:21840320};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00172,
CC ECO:0000269|PubMed:21840320};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=0.0096 umol/min/mg enzyme with tetrahydrofolate as substrate (at
CC pH 4.6 and 37 degrees Celsius) {ECO:0000269|PubMed:21840320};
CC Vmax=0.125 umol/min/mg enzyme with tetrahydrofolate as substrate (at
CC pH 5.0 and 37 degrees Celsius) {ECO:0000269|PubMed:21840320};
CC Vmax=0.135 umol/min/mg enzyme with tetrahydrofolate as substrate (at
CC pH 5.5 and 37 degrees Celsius) {ECO:0000269|PubMed:21840320};
CC Vmax=0.152 umol/min/mg enzyme with tetrahydrofolate as substrate (at
CC pH 6.0 and 37 degrees Celsius) {ECO:0000269|PubMed:21840320};
CC Vmax=0.155 umol/min/mg enzyme with tetrahydrofolate as substrate (at
CC pH 6.5 and 37 degrees Celsius) {ECO:0000269|PubMed:21840320};
CC Vmax=0.148 umol/min/mg enzyme with tetrahydrofolate as substrate (at
CC pH 7.0 and 37 degrees Celsius) {ECO:0000269|PubMed:21840320};
CC Vmax=0.146 umol/min/mg enzyme with tetrahydrofolate as substrate (at
CC pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:21840320};
CC Vmax=0.150 umol/min/mg enzyme with tetrahydrofolate as substrate (at
CC pH 8.0 and 37 degrees Celsius) {ECO:0000269|PubMed:21840320};
CC Vmax=0.146 umol/min/mg enzyme with tetrahydrofolate as substrate (at
CC pH 8.5 and 37 degrees Celsius) {ECO:0000269|PubMed:21840320};
CC Vmax=0.119 umol/min/mg enzyme with tetrahydrofolate as substrate (at
CC pH 9.0 and 37 degrees Celsius) {ECO:0000269|PubMed:21840320};
CC pH dependence:
CC Optimum pH is between 6-8. Outside of this pH range, the enzyme
CC activity decreases rapidly. At pH 4.6, the enzyme is only 7% as
CC active as it is at pH 7.5. {ECO:0000269|PubMed:21840320};
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, ECO:0000269|PubMed:21840320}.
CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC family. {ECO:0000255|HAMAP-Rule:MF_00172}.
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DR EMBL; AE014133; AAN58588.1; -; Genomic_DNA.
DR RefSeq; NP_721282.1; NC_004350.2.
DR RefSeq; WP_002262021.1; NC_004350.2.
DR PDB; 2NQ5; X-ray; 1.90 A; A=2-745.
DR PDB; 3L7R; X-ray; 2.40 A; A=1-745.
DR PDB; 3T0C; X-ray; 2.19 A; A=1-745.
DR PDBsum; 2NQ5; -.
DR PDBsum; 3L7R; -.
DR PDBsum; 3T0C; -.
DR AlphaFoldDB; Q8CWX6; -.
DR SMR; Q8CWX6; -.
DR STRING; 210007.SMU_873; -.
DR PRIDE; Q8CWX6; -.
DR EnsemblBacteria; AAN58588; AAN58588; SMU_873.
DR KEGG; smu:SMU_873; -.
DR PATRIC; fig|210007.7.peg.779; -.
DR eggNOG; COG0620; Bacteria.
DR HOGENOM; CLU_013175_0_0_9; -.
DR OMA; KVMKGML; -.
DR PhylomeDB; Q8CWX6; -.
DR BRENDA; 2.1.1.14; 5941.
DR UniPathway; UPA00051; UER00082.
DR EvolutionaryTrace; Q8CWX6; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 3D-structure; Amino-acid biosynthesis; Metal-binding;
KW Methionine biosynthesis; Methyltransferase; Reference proteome; Repeat;
KW Transferase; Zinc.
FT CHAIN 1..745
FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT methyltransferase"
FT /id="PRO_0000098670"
FT ACT_SITE 683
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 19
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 115
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 420..422
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 420..422
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 473
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 473
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 478
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 501
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 504..505
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 550
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 588
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 588
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 630
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172,
FT ECO:0000269|PubMed:21840320, ECO:0007744|PDB:3T0C"
FT BINDING 632
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172,
FT ECO:0000269|PubMed:21840320, ECO:0007744|PDB:3T0C"
FT BINDING 654
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:21840320,
FT ECO:0007744|PDB:3T0C"
FT BINDING 715
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00172,
FT ECO:0000269|PubMed:21840320, ECO:0007744|PDB:3T0C"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 32..52
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 170..190
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 252..261
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:2NQ5"
FT TURN 271..276
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:3L7R"
FT HELIX 294..306
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 308..317
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 343..357
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 364..376
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 399..410
FT /evidence="ECO:0007829|PDB:2NQ5"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:3T0C"
FT HELIX 444..464
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 481..484
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 510..517
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 523..531
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 537..542
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 544..550
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 559..579
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 584..589
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 592..595
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 600..618
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 625..631
FT /evidence="ECO:0007829|PDB:2NQ5"
FT TURN 637..639
FT /evidence="ECO:0007829|PDB:3T0C"
FT HELIX 640..646
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 649..653
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 656..658
FT /evidence="ECO:0007829|PDB:3T0C"
FT HELIX 661..663
FT /evidence="ECO:0007829|PDB:3T0C"
FT HELIX 664..668
FT /evidence="ECO:0007829|PDB:3T0C"
FT STRAND 674..678
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 690..698
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 699..702
FT /evidence="ECO:0007829|PDB:2NQ5"
FT HELIX 706..708
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 709..712
FT /evidence="ECO:0007829|PDB:2NQ5"
FT STRAND 717..720
FT /evidence="ECO:0007829|PDB:3L7R"
FT HELIX 722..741
FT /evidence="ECO:0007829|PDB:2NQ5"
SQ SEQUENCE 745 AA; 84141 MW; 9CD5B8905192D823 CRC64;
MTKVSSLGYP RLGENREWKK LIEAYWAGKV SKNDLFAGAK ELRLDFLKKQ LNAGLDLIPV
GDFSLYDHIL DLSVQFNIIP KRFAKEPIDI DLYFAIARGN KENVASSMKK WFNTNYHYIV
PEWSKQRPKL NNNRLLDLYL EAREVVGDKA KPVITGPITY VALSTGVEDF TAAVKSLLPL
YKQVFTELVK AGASYIQVDE PIFVTDEGKD YLQAAKAVYA YFAKEVPDAK FIFQTYFEGL
IDSQVLSQLP VDAFGLDFVY GLEENLEAIK TGAFKGKEIF AGVIDGRNIW SSDFVKTSAL
LETIEEQSAA LTIQPSCSLL HVPVTTKNET DLDPVLRNGL AFADEKLTEV KRLAEHLDGR
EDPAYDLHIA HFDALQAADF RNVKLEDLSR VATKRPSDFA KRRDIQQEKL HLPLLPTTTI
GSFPQSREIR RTRLAWKRGD ISDAEYKQFI QAEIERWIRI QEDLDLDVLV HGEFERVDMV
EFFGQKLAGF TTTKFGWVQS YGSRAVKPPI IYGDVQHLEP ITVEETVYAQ SLTDRPVKGM
LTGPITITNW SFERTDIPRD QLFNQIGLAI KDEIKLLENA GIAIIQVDEA ALREGLPLRK
SKQKAYLDDA VHAFHIATSS VKDETQIHTH MCYSKFDEII DAIRALDADV ISIETSRSHG
DIIESFETAV YPLGIGLGVY DIHSPRVPTK EEVVANIERP LRQLSPTQFW VNPDCGLKTR
QEPETIAALK VLVAATKEVR QKLGN
